H. Peter Lu

lu4H. Peter Lu, Ph.D.

Ohio Eminent Scholar and Professor, Chemistry Dept.
021 Overman Hall
419.372.1840
hplu@bgsu.edu

Lu's Group

Current Activities and Projects

Single-molecule spectroscopy study of interfacial electron transfer dynamics, protein-protein interaction dynamics, enzymatic reaction dynamics, and ion-channel protein dynamics.

Research Interests

My research (Current Research Scope) involves single-molecule spectroscopy studies of molecular kinetics and dynamics in condensed phase and at interfaces. Research on the single-molecule/nanoparticle interfacial electron transfer dynamics represents an applications of single-molecule approaches to study an important interfacial chemical reaction that was traditionally studied by ensemble-averaged experiments. We have been applying single-molecule fluorescence and surface-enhanced Raman spectroscopies to obtain detailed Franck-Condon vibronic coupling, electron-transfer driving forces, and solvent relaxation energies of electron donor molecules and the nanoparticles. In the area of reaction and dynamics in proteins and protein complexes, we are studying the dynamics and mechanisms of single-molecule enzymatic reactions and non-covalent DNA-protein and protein-protein interactions. Non-Arrhenius and non-Markovian dynamics, allosteric effect, cooperativity, and memory effects of enzymatic reactions have been widely observed but are poorly understood due to the nature of the static and dynamic inhomogeneities in an ensemble-averaged measurement as well as in the intrinsic molecular dynamics. By applying single-molecule approaches, we have been able to investigate the protein conformational relaxation and fluctuation behaviors to identify the protein conformational motion dynamics and the correlated enzymatic turnover dynamics and mechanisms. Our research has also provided unique experimental identifications and characterizations of fluctuating noncovalent protein-protein interactions in cell signaling and protein-DNA interactions in DNA damage recognition. These fluctuating and inhomogeneous conformational motions in protein-protein and protein-DNA complexes most likely determine the capability of protein recognitions and DNA damage recognition. We also developed a number of AFM-tip enhanced NSOM fluorescence and Raman optical imaging approaches that are capable of obtaining Raman or fluorescence imaging beyond optical diffraction limited spatial resolution. We had applied our AFM-tip enhanced or correlated optical imaging approaches to analyzing bacterial cell membrane proteins.

Cell signaling is at the core of most biological functions and often involves dynamic interactions among proteins. Protein-protein interactions induce conformational changes that initiate chain reactions, which in turn lead to cellular responses. A comprehensive understanding of such protein interactions is crucial to understanding the regulatory mechanisms controlling cellular functions. To study protein interactions in cell signaling, ensemble measurements, which yield information only on averaged properties, are inadequate. Intrinsically, the crucial early events of cell signaling often involve only a few molecules and then are magnified along the signaling pathways. Moreover, for intrinsically heterogeneous systems such as protein complexes, protein interaction dynamics contain static and dynamic disorders as a result of spatial and temporal inhomogeneities. Stochastic protein-protein interactions prevent such characterizations when many molecules are measured simultaneously. Single-molecule spectroscopy is crucial to obtaining such information because it is capable of characterizing biomolecular processes that are inhomogeneous and non-synchronizable. We have conducted a single-molecule study of protein-protein interaction dynamics in an intracellular signaling protein complex, Cdc42/WASP, employing a novel CBD biosensor, which is a dye-labeled WASP fragment that binds only the GTP-activated Cdc42, we were able to probe hydrophobic interactions associated with Cdc42/WASP recognition. Single-molecule fluorescence measurements indicated static and dynamic disorders in this protein-protein interaction system, and our study characterized the dynamic and inhomogeneous nature of molecular recognition within the Cdc42/WASP signaling complex. A coupled-two channel fluctuation Markovian model was proposed for the fluctuation dynamics, and the molecular structure and solvent-accessible surface of the protein-protein interaction complex were explored by MD simulations. The Cdc42-CBD complexes showed conformational fluctuations between bound and loosely bound states while the overall complex was still associated. The distribution of the fluctuation rates was highly inhomogeneous, with variations among individual complexes of two orders of magnitude under the same conditions. The results suggest highly dynamic rather than static protein-protein interactions in this cell signaling system. Such dynamic and fluctuating protein-protein interactions may be important for inducing and regulating downstream signaling events. By establishing a molecular imaging system with adequate spatial and temporal resolution and combining single-molecule experimental and computational approaches, we expect to expand our studies to other important biomolecular complexes under physiological conditions and eventually to living cells.

Complex conformational changes influence and regulate the dynamics of ion channels in living cells. Such conformational changes are stochastic and often inhomogeneous, which makes it extremely difficult, if not impossible, to characterize them by ensemble-averaged experiments or by single-channel recordings of the electric current that report the open-closed events but do not specifically probe the associated conformational changes. We have conducted studies on ion channel conformational changes using a new approach, patch-clamp fluorescence microscopy (PCFM), which simultaneously combines single-molecule fluorescence spectroscopy and single-channel current recordings to probe the open-closed transitions and the conformational dynamics of individual ion channels. We demonstrated PCFM by measuring gramicidin ion channel conformational changes in a lipid bilayer formed at a patch-clamp micropipette tip under a buffer solution. By measuring single-pair fluorescence resonance energy transfer (spFRET) and fluorescence self-quenching from dye-labeled gramicidin channels, we observed that the efficiency of spFRET and self-quenching is widely distributed, which reflects a broad distribution of conformations, including "silent" states of active channels. Our results strongly suggest a hitherto undetectable correlation between the multiple conformational states of the gramicidin channel and its closed and open states in a lipid bilayer. We have recently applied this new single-molecule experimental approach for studying ion-channel conformational dynamics and mechanisms of NMDA receptors in living cells.

As a crucial and early event in the DNA repair process, DNA damage recognition involves complex protein-DNA and protein-protein interactions. Our single-molecule spectroscopy study reveals dynamics of fluctuating molecular non-covalent interactions within single XPA-DNA complexes that are involved in the DNA (NER) damage recognition processes. These results have facilitated a molecule-level understanding of the dynamics and mechanisms of the damage-recognition process in DNA repair. We observed fluorescence-intensity fluctuations in single XPA-DNA complexes at two different time-scales. We concluded that the fast conformational change coordinates are associated with DNA structural fluctuations, but slow conformational coordinates are attributed to interactive motions of the XPA-DNA complex at the binding site, a finding consistent with XPA’s ability to recognize a wide variety of DNA lesions. The required, slow and large-amplitude conformational motions of XPA-DNA complexes have not been reported previously. Approximately 10-fold variation occurs in the rates of the slow interactive conformational motions among the individual complexes. This inhomogeneity is most likely associated with the existence of different subsets of protein conformations seeking an induced-fit to a conformationally fluctuating DNA lesion. Conformational dimensionality reduction, fly-casting driven by induced-fit, water and ion exclusion, DNA and peptide chain diffusive relaxation, protein interior packing relaxation, and hydrogen bond formations are all likely associated with the potential barriers for the trapped interactive states. These trapped and slow-fluctuating interactions could be crucial in XPA-DNA interaction dynamics and intrinsically pertinent to the protein-DNA complexes in other DNA damage recognition processes.

We have applied single-molecule spectroscopy and ultrafast spectroscopy on single molecule studies of photosensitized interfacial electron transfer (ET) processes in Coumarin 343 (C343)-TiO2 nanoparticle (NP) and Cresyl Violet (CV+)-TiO2 NP systems, using time-correlated single photon counting coupled with scanning confocal fluorescence microscopy. Fluorescence intensity trajectories of individual dye molecules adsorbed on a semiconductor NP surface showed fluorescence fluctuations and blinking, with time constants distributed from milliseconds to seconds. The fluorescence fluctuation dynamics were found to be inhomogeneous from molecule to molecule and from time to time, showing significant static and dynamic disorders in the interfacial ET reaction dynamics. We attribute fluorescence fluctuations to the interfacial ET reaction rate fluctuations, associating redox reactivity intermittency with the fluctuations of molecule-TiO2 electronic and Franck-Condon coupling. The inhomogeneous nanoscale molecule-surface and molecule-molecule interactions are presumably the origins of the complexity in interfacial ET dynamics. These nanoscale inhomogenities at interfaces or on surfaces make it highly difficult for ensemble-averaged measurements to dissect the complex interfacial ET processes. The difficulty comes from both spatial and temporal inhomogeneities, which can be identified, measured, and analyzed best by studying one molecule at a time in a specific nanoscale local environment. Intermittent interfacial ET dynamics of individual molecules could be characteristic of a surface chemical reaction strongly involved with and regulated by molecule-surface interactions. The intermittent interfacial reaction dynamics that likely occur among single molecules in other interfacial and surface chemical processes can typically be observed by single-molecule studies, but not by conventional ensemble-averaged experiments.

Single-molecule fluorescence intensity trajectories contain rich information about the molecular dynamics of protein conformational changes, DNA-protein interactions, and protein-protein interactions. However, the typical dynamic range of the single-molecule trajectories has only been from the sub-millisecond to second-and-longer. We have developed single-molecule spectroscopic capabilities to measure the single-molecule fluorescence lifetime trajectories, extending the time scale to the nanosecond regime. At the same time, we have initiated methods to obtain single molecule fluorescence anisotropy trajectories at the nanosecond-to-second time-scale and to achieve a nanoscale topographic characterization in correlations with single-molecule spectroscopy.

Single-Molecule Time-Resolved Fluorescence Anisotropy: Molecule rotational motion rates are dependent upon molecular hydrodynamic shapes and masses that can be changed by molecular interactions and complex formation/dissociation. Measuring the time-dependent anisotropy of a site-specifically labeled dye molecule would be a means of probing the conformational motions of the labeled domain of the protein. Because the time-scale for dye molecule spinning is in the sub-nanosecond range, the nanosecond-to-microsecond protein conformational motions can be differentiated and probed by measuring the time-dependent anisotropy of the dye molecules in this longer time regime. The results will be observed as changes in the fluorescence polarization anisotropy in time. This technique allows us to measure the single-molecule conformational changes as well as the substrate-enzyme complex formation, reaction, and dissociation in real time.

AFM-enhanced optical spectroscopic microscopy: We have been working to combine AFM and single-molecule microscopy in one instrument in order to obtain molecular scale topographic information and the correlated spectroscopic information for the same single-molecule reaction system. This approach enhances research in our protein conformational and enzymatic reaction dynamics project. Single-molecule dynamics have been "traditionally" studied using fluorescence spectroscopy that probes the overall molecular or active site conformational fluctuations and the excited-state lifetimes. Vibrational-mode resolved single-molecule dynamics has never been conducted due to the lack of vibrational specificity of fluorescence. Quite conceivably, Raman spectroscopy, including surface-enhanced Raman spectroscopy (SERS), could provide rich information on vibrational relaxation, vibrational coupling, chemical bond formation/dissociation, and mode-specific nuclear displacements. Based on the near-field enhancement at the metallic AFM tip, we have experimentally demonstrated AFM tip enhanced fluorescence lifetime imaging microscopy (AFM-FLIM) and currently working on demonstrating the AFM tip enhanced surface enhanced Raman spectroscopy (AFM-SERS) imaging guided by finite element method (FEM) computational simulation of the near-field electronmagnetic field distributions.

Past Experience

  • Ohio Board of Regents Eminent Scholar and Professor, Bowling Green State University, 2006 - present
  • Chief Scientist, Pacific Northwest National Laboratory, 2005-2006
  • Senior Research Scientist II, Pacific Northwest National Laboratory, 1999-2005
  • Senior Research Scientist, Pacific Northwest National Laboratory, 1996-1999
  • Postdoctoral Fellow, Pacific Northwest National Laboratory, 1995-1996
  • Postdoctoral Research Associate, Northwestern University, 1991-1995
  • Assistant Professor of Physical Chemistry, Peking University, 1984-1986

Education

  • Columbia University, Ph.D. Chemistry, 1991
  • Columbia University, M. Phil. Chemistry, 1989
  • Peking University, M. Sci. Chemistry, 1984
  • Peking University, B.A. Chemistry, 1982

Awards, Honors, & Appointments

  • BGSU Teaching Award, BGSU, 2019-2020
  • Elected an American Physical Society Fellow, 2014
  • Olscamp Research Award, BGSU, 2009
  • FSD Outstanding Performance Award, PNNL, 2004
  • FSD Outstanding Performance Award, PNNL, 2003
  • FSD Outstanding Performance Award, PNNL, 2002
  • FSD Outstanding Performance Award, PNNL, 2001
  • ESHD Outstanding Performance Award, PNNL, 1999

Selected Recent Publications

  1. Sunidhi Jaiswal, Xiaonan Han, and H. Peter Lu, "Probing Protein-DNA Conformational Dynamics in DNA Damage Recognition: XPA Stabilizes Damaged DNA-RPA14 Complex by Controlling Conformational Fluctuation Dynamics," J. Phys. Chem. B, 126, 997-1003 (2022).

  2. Sunidhi Jaiswal, Yufan He, and H. Peter Lu, "Probing Functional Conformation-State Fluctuation Dynamics in Recognition Binding between Calmodulin and Target Peptide," J. Chem. Phys., 156, 055102 (2022).

  3. S. Roy Chowdhury, H. Peter Lu, "Unraveling the Mechanism of Tau Protein Aggregation in Presence of Zinc Ion: The Earliest Step of Tau Aggregation," Chem. Phys. Impact, 4, 100060 (2022)

  4. Yufan He, Mohammad Mahfuzul Haque, Dennis J. Stuehr, H. Peter Lu, "Conformational States Fluctuations in Endothelial Nitric Oxide Synthase under Calmodulin Regulation," Biophys. J., 120, 1-11 (2021).

  5. Meiling Wu, H. Peter Lu, "Ultra-Sensitive Lock-in Amplifier Coupled Oscillatory Magnetic Tweezers for PicoNewton Force Manipulation Applications," Feature Article, J. Applied Physics, 130, 014504 (2021).

  6. Kaustav Dey, S. Roy Chowdhury, Erik Dykstra, H. Peter Lu, Ruth Shinar, Joseph Shinar, and Pavel Anzenbacher, Jr., "Effect of Bis-diazirine-Mediated Photo-Crosslinking on Polyvinylcarbazole and Solution-Processed Polymer LEDs," ACS Applied Electronic Materials, 3, 3365-3371 (2021).

  7. K. Dey, S. R. Chowdhury, E. Dykstra, A. Koronatov, H. P. Lu, R. Shinar, J. Shinar, P. Anzenbacher, "Diazirine-Based Photo-Crosslinkers for Defect Free Fabrication of Solution Processed Organic Light-Emitting Diodes," Journal of Materials Chemistry C, 8, 11988-11996 (2020).

  8. S. Roy Chowdhury, Sunidhi Jaiswal, H. Peter Lu, "Compressive-force induced activation of apo-calmodulin in protein signaling," Physical Chemistry Chemical Physics, 22, 1092-1096 (2020).

  9. S. Roy Chowdhury, H. Peter Lu, "Spontaneous Rupture and Entanglement of Human Neuronal Tau Protein Induced by Piconewton Compressive Force," ACS Chemical Neuroscience, 10, 4061-4067 (2019).

  10. Meiling Wu, H. Peter Lu, "Oscillating picoNewton Force Manipulation on Single-Molecule Enzymatic Conformational and Reaction Dynamics" J. Phys. Chem. B, 122, 12312-12321 (2018).

  11. Achut P. Silwal, H. Peter Lu, "Raman Spectroscopic Analysis of Signaling Molecules-Dopamine Receptors Interaction in Living Cells," ACS Omega , 3, 14849-14857 (2018).

  12. Achut P. Silwal, H. Peter Lu, "Mode-Selective Raman Imaging of Dopamine-Human Dopamine Transporter Interaction in Live Cells," ACS Chemical Neuroscience, 9, 3117-3127 (2018).

  13. Zijiang Wang, H. Peter Lu, "Single-Molecule Spectroscopy Study of Crowding-Induced Protein Spontaneous Denature and Crowding-Perturbed Unfolding-Folding Conformational Fluctuation Dynamics," J. Phys. Chem. B, 122, 6724-6732 (2018).

  14. Achut P. Silwal, H. Peter Lu, "Raman Spectroscopy Probing of Redox States and Mechanism of Flavin Coenzyme," J. Raman Spectrosc., 49, 1311-1322 (2018).

  15. S. Roy Chowdhury, H. Peter Lu, "Probing Activated and Non-Activated Single Calmodulin Molecule under a picoNewton Compressive Force," Biochemistry, 57, 1945-1948 (2018).

  16. S. Roy Chowdhury, Jin Cao, Yufan He, and H. Peter Lu, "Revealing Abrupt and Spontaneous Ruptures of Protein Native Structure under Pico-Newton Compressive Stress Force Manipulation," ACS Nano, 12, 2448-2454 (2018).

  17. J. Wang, S. Xia, J. Bi, M. Fang, W. Mazi, Y. Zhang, N. Conner, F. Luo, H. Peter Lu, Haiying Liu, "Ratiometric Near-infrared Fluorescent Probes Based on TBET and p-Conjugation Modulation between Tetraphenylethene and Hemicyanine Moieties for Sensitive Detection of pH Changes in Live Cells," Bioconjugate Chemistry, 29, 1406-1418 (2018).

  18. Rajeev Yadav, and H. Peter Lu, "Probing the Dynamic Heterogeneity in the Aggregated Ion Channels in Live Cells," J. Phys. Chem. C, 122, 13716-13723 (2018).

  19. Rajeev Yadav, and H. Peter Lu, "Revealing Dynamically-Organized Receptor Ion Channel Clusters in Live Cells by a Correlated Electric Recording and Super-Resolution Single-Molecule Imaging," Phys. Chem. Chem. Phys., 20, 8088-8098 (2018).

  20. Lingci Zhao, H. Peter Lu, and Jin Wang, "Exploration of Multistate Conformational Dynamics upon Ligand Binding of a Monomeric Enzyme Involved in Pyrophosphoryl Transfer," J. Phys. Chem. B, 122, 1885-1897 (2018).

  21. Meiling Wu, Rajeev Yadav, Nibedita Pal, and H. Peter Lu, "Manipulating Motions of Targeted Single Cells in Solution by an Integrated Double-Ring Magnetic Tweezers Imaging Microscope," Rev. Sci. Instrum., 88, 07373 (2017).

  22. Bharat Dhital, Vishal Govind Rao, and H. Peter Lu, "Probing Single-Molecule Electron-Hole Transfer Dynamics at a Molecule-NiO Semiconductor Nanocrystalline Interface," Phys. Chem. Chem. Phys., 19, 17216-17223 (2017).

  23. Achut P. Silwal, Rajeev Yadav, Jon E. Sprague, and H. Peter Lu, "Raman Spectroscopic Signature Markers of Dopamine-Human Dopamine Transporter Interaction in Living Cells," ACS Chemical Neuroscience, 8, 1510-1518 (2017).

  24. Fei Liu, Xiakun Chu, H. Peter Lu, and Jin Wang, "Molecular mechanism of multispecific recognition of Calmodulin through conformational changes," Proc. Natl. Acad. Sci., 114, E3927-E3934 (2017).

  25. Maolin Lu, H. Peter Lu, "Revealing Multiple Pathways in T4 Lysozyme Substep Conformational Motions by Single-Molecule Enzymology and Modeling," J. Phys. Chem. B, 121, 5017-5024 (2017).

  26. Pavel Moroz, Natalia Razgoniaeva, Yufan He, Gregory Jensen, Holly Eckard, H. Peter Lu, and Mikhail Zamkov, "Tracking the Energy Flow on Nanoscale via Sample-Transmitted Excitation Photoluminescence Spectroscopy," ACS Nano, 11, 4191-4197 (2017).

  27. Nibedita Pal, Meiling Wu, H. Peter Lu, "Probing Conformational Dynamics of Enzymatic Active Site by an In Situ Single Fluorogenic Probe under picoNewton Force Manipulation," Proc. Natl. Acad. Sci., 113, 15006-15011 (2016).

  28. Vishal G. Rao, H. Peter Lu, "Inhomogeneous and Complex Interfacial Electron-Transfer Dynamics: A Single-Molecule Perspective," ACS Energy Lett., invited review article, 1, 773-791 (2016).

  29. Dibyendu Sasmal, Rajeev Yadav, H. Peter Lu, "Single-Molecule Patch-Clamp-FRET-Anisotropy Microscopy Studies of NMDA Receptor Ion Channel Activation and Deactivation under Agonist Ligand Binding in Living Cells," J. Am. Chem. Soc., 138, 8789-8801 (2016).

  30. Yufan He, Vishal G. Rao, Jin Cao, H. Peter Lu, "Simultaneous Spectroscopic and Topographic Imaging of Single-Molecule Interfacial Electron Transfer Reactivity and Local Nanoscale Environment," J. Phys. Chem. Lett., 7, 2221-2227 (2016).

  31. Bharat Dhital, Vishal G. Rao, H. Peter Lu, "Electronic Coupling-Decoupling Dependent Single-Molecule Interfacial Electron Transfer Dynamics in Electrostatically-Attached Porphyrin on TiO2 Nanoparticles," J. Phys. Chem. C, 120, 12313-12324 (2016).

  32. Min Gu, H. Peter Lu, "Raman Mode-Selective Spectroscopic Imaging of Coenzyme and Enzyme Redox States," J. Raman Spectrosc., 47, 801-807 (2016).

  33. Arthur Yu, Shaowei Li, Bharat Dhital, H. Peter Lu, Wilson Ho, "Tunneling Electron Induced Charging and Light Emssion of Single Panhematin Molecules," J. Phys. Chem. C, 120, 21099-21103 (2016).

  34. Papatya Sevinc, Bharat Dhital,Vishal G. Rao,Yuanmin Wang, H. Peter Lu, "Probing Electric Field Effect on Covalent Interactions at a Molecule-Semiconductor Interface" J. Am. Chem. Soc., 138,1536-1542 (2016). Link

  35. Vishal G. Rao, Bharat Dhital, H. Peter Lu, "Probing Driving Force and Electron Accepting State Density Dependent Interfacial Electron Transfer Dynamics: Suppressed Fluorescence Blinking of Single-Molecules on Indium Tin Oxide Semiconductors," J. Phys. Chem. B., 120,1685-1697 (2016). Link

  36. Suneth P. Rajapaksha, Nibedita Pal, Desheng Zheng, H. Peter Lu, "Protein-fluctuation-induced water-pore formation in ion channel voltage-sensor translocation across a lipid bilayer membrane," Phys. Rev. E, 92, 052719 (2015). Link

  37. Qing Guo, Yufan He, H. Peter Lu, "Interrogating the Activities of Conformational Deformed Enzyme by Single Molecule Fluorescence-Magnetic Tweezers Microscopy," Proc. Natl. Acad. Sci., 112,13904-13909 (2015). Link

  38. Vishal G. Rao, Bharat Dhital, H. Peter Lu, "Single-Molecule Interfacial Electron Transfer Dynamics of Porphyrin on TiO2 Nanoparticles: Dissecting Interfacial Electric Field and Electron Accepting State Density Dependent Dynamics ," Chem. Commun., 51,16821-16824 (2015). Link

  39. Zhoufeng Jiang, Ghadendra B. Bhandari,Shashini Premathilake, Simeen Khanh, Douglas M. Dimick, Cody Stombaugh, Angelic Mandell, Yufan He, H. Peter Lu and Liangfeng Sun, "Growth of colloidal PbS nanosheets and the enhancement of their photoluminescence," Phys. Chem. Chem. Phys., 17, 23303 (2015). Link

  40. Yufan He, Mohammad Mahfuzul Haque, Dennis J. Stuehr, H. Peter Lu, "Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics," Proc. Natl. Acad. Sci., 112, 11835-11840 (2015). Link

  41. Zijinag Wang, H. Peter Lu, "Probing Single-Molecule Protein Spontaneous Folding-Unfolding Conformational Fluctuation Dynamics: The Multiple-State and Multiple-Pathway Energy Landscape," J. Phys. Chem. B., 119, 6366-6378 (2015). Link

  42. Valentina Brega, Matthias Zeller, Yufan He, H. Peter Lu and Jeremy K. Klosterman, "Multi-Responsive Metal-Organic Lantern Cages in Solution," Chem. Commun., 51,5077-5080 (2015). Link

  43. Maolin Lu, H. Peter Lu, "Probing Protein Multi-Dimensional Conformational Fluctuations by Single-Molecule Multi-Parameter Photon Stamping Spectroscopy," J. Phys. Chem. B., 118,11943-11955 (2014).Link

  44. Dibyendu Kumar Sasmal, H. Peter Lu, " Single-Molecule Patch-Clamp FRET Microscopy Studies of NMDA Receptor Ion Channel Dynamics in Living Cells: Revealing the Multiple Conformational States Associated with a Channel at Its Electrical Off State," J. Am. Chem. Soc., 136, 12998-13005 (2014).Link

  45. Ghadendra B. Bhandari, Kamal Subedi, Yufan He, Zhoufeng Jiang, Matthew Leopold, Nick Reilly, H. Peter Lu, Alexey T. Zayak and Liangfeng Sun, "Thickness-Controlled Synthesis of Colloidal PbS Nanosheets and Their Thickness-Dependent Energy Gaps", Chemistry of Materials , 26, 5433-5436 (2014).Link

  46. Vishal Govind Rao, Bharat Dhital, Yufan He, H. Peter Lu, " Single-Molecule Interfacial Electron Transfer Dynamics of Porphyrin on TiO2 Nanoparticles: Dissecting the Complex Electronic Coupling Dependent Dynamics," J. Phys. Chem. C., 118, 20209-20221 (2014). Link

  47. Desheng Zheng, H. Peter Lu, " Single-Molecule Enzymatic Conformational Dynamics: Spilling Out the Product Molecules,"J. Phys. Chem. B., 118, 9128-9140 (2014). Link

  48. Qing Guo, Yufan He, H. Peter Lu, "Repetitive Force Pulling-Releasing Manipulation of Enzymatic Conformational Fluctuations and Enzyme-Substrate Interactions by Single-Molecule FRET-Magnetic Tweezers Microscopy," Phys. Chem. Chem. Phys., 16, 13052 -13058 (2014). Link

  49. H. Peter Lu, " Single-Molecule Interfacial Electron Transfer Dynamics," an invited book chapter in Handbook of Spectroscopy, Second Edition ( G. Gauglitz and D. S. Moore. Eds), p. 877-910, Wiley-VCH Verlag GmbH & Co. (2014). Link

  50. H. Peter Lu, “Sizing up single-molecule enzymatic conformational dynamics,” Chem. Soc. Rev., Invited Review Article, 43, 1118-1143 (2014). Link

  51. Suneth P. Rajapaksha, Xuefei Wang, H. Peter Lu, “Suspended Lipid Bilayer for Optical and Electrical measurements of Single Ion Channel Proteins,” Anal. Chem., 85, 8951-8955 (2013). Link

  52. Suneth P. Rajapaksha, Yufan He, H. Peter Lu, “Combined Topographic, Spectroscopic, and Model Analyses of Inhomogeneous Energetic Coupling of Linear Light Harvesting Complex II Aggregates in Native Photosynthetic Membrane,” Phys. Chem. Chem. Phys., 15, 5636-5647 (2013). Link

  53. Qian Wang, Yuanmin Wang, H. Peter Lu, “Revealing the Secondary Structural Changes of Amyloid β Peptide by Probing the Spectral Fingerprint Characters,” J. Raman Spectroscopy, 44, 670-674 (2013). Link

  54. Yuanmin Wang, Papatya Sevinc, Sara Balchik, Jim Fridrickson, Liang Shi, H. Peter Lu, “Single-Cell Imaging and Spectroscopic Analyses of Cr(VI) Reduction on the Surface of Bacterial Cells,” Langmuir, 29, 950-956 (2013). Link

  55. Yufan He, Maolin Lu, H. Peter Lu, “Single-Molecule Photon Stamping FRET Spectroscopy Study of Enzymatic Conformational Dynamics,” Phys. Chem. Chem. Phys., 15, 770-775 (2013) (Cover page). Link

  56. Yufan He, Maolin Lu, Jin Cao, H. Peter Lu, “Manipulating Protein Conformations by Single-Molecule AFM-FRET Nanoscopy,” ACS Nano6, 1221-1229 (2012). Link

  57. H. Peter Lu, “Enzymes in Coherent Motion,” Science, 335, 300-301 (2012). Link

  58. Desheng Zheng, Leonora Kaldaras, H. Peter Lu , “Total Internal Reflection Fluorescence Microscopy Imaging-Guided Confocal Single-Molecule Fluorescence Spectroscopy,” Review of Scientific Instruments, 83, 013110 (2012). Link

  59. He, Yufan; Li, Yue; Mukherjee, Saptarshi; Wu, Yan; Yan, Honggao; Lu, H. Peter, "Probing Single-Molecule Enzyme Active-Site Conformational State Intermittent Coherence," J. Am. Chem. Soc. 133, 14389-14395 (2011). Link

  60. Suraj Saraswat, Anil Desireddy, Desheng Zheng, Lijun Guo, H. Peter Lu, Terry P. Bigioni, and Dragan Isailovic, “Energy Transfer from Fluorescent Proteins to Metal Nanoparticles,” J. Phys. Chem. C 115(35), 17587-17593 (2011). Link

  61. X. Wang, D. Zhang, Y. Wang, P. Sevinc, H. Peter, Lu, A. J. Meixner,   “Interfacial Electron Transfer Energetics Studied by High Spatial Resolution Tip-Enhanced Raman Spectroscopic Imaging,” Angewandte Chemie International Edition 50, (2011) A25-A29. Link

  62. Sara M. Belchik, David W. Kennedy, Alice C. Dohnalkova, Yuanmin Wang, Papatya C. Sevinc, Hong Wu, Yuehe Lin, H. Peter Lu, James K. Fredrickson, and Liang Shi, “Extracellular Reduction of Hexavalent Chromium by MtrC and OmcA of Shewanella oneidensis MR-1,”  Applied and Environmental Microbiology, 77, 4035-4041 (2011). Link

  63. Yuanmin Wang, Papatya C. Sevinc, Yufan He, H. Peter Lu, " Probing Ground-State Single-Electron Self-Exchange Across a Molecule-Metal Interface," J. Am. Chem. Soc., 133, 6989-6996 (2011). Link

  64. H. Peter Lu, "Revealing Time Bunching Effect in Single-Molecule Enzyme Conformational Dynamics," Phys. Chem. Chem. Phys., 13, 6734-6749 (2011). Link

  65. Sevinc, Papatya; Wang, Xiao; Wang, Yuanmin; Zhang, Dai; Meixner, Alfred; Lu, H. Peter, "Simultaneous Spectroscopic and Topographic Near-Field Imaging of TiO2 Single Surface States and Interfacial Electronic Coupling," Nano Letters, 1490-1494 (2011). Link

  66. Yuanmin Wang, H. Peter Lu, "Bunching Effect in Single-Molecule T4 Lysozyme Non-Equilibrium Conformational Dynamics under Enzymatic Reactions," J. Phys. Chem. B, 114, 6669-6674 (2010) (Cover page)Link
     
  67. H. Peter Lu, "Acquiring a Nano-View of Single Molecules in Actions," Nano Reviews 1, 6-7 (2010). Link

  68. H. Peter Lu, "Single-Molecule Protein Conformational Dynamics in Enzymatic Reactions," Chapter 24, PP471-494 in Single Molecule Spectroscopy in Chemistry, Physics and Biology: Nobel Symposium (Springer Publishing, 2010). Link

  69. Guo, Lijun; Wang, Yuanmin; Lu, H. Peter, "Combined Single-Molecule Photon-Stamping Spectroscopy and Femtosecond Transient Absorption Spectroscopy Studies of Interfacial Electron Transfer Dynamics," J. Am. Chem. Soc. 132, 1999-2004 (2010) (Cover page). Link

  70. Yufan He, Xiaohua Zeng, Saptarshi Mukherjee, Suneth Rajapaksha, Samuel Kaplan, H. Peter Lu, "Revealing Linear Aggregates of Light Harvesting Antenna Proteins in Photosynthetic Membranes," Langmuir 26, 307-313 (2010) (Cover page)Link

  71. Yuanmin Wang, Xuefei Wang, and H. Peter Lu, "Probing single-molecule interfacial geminate electron-cation recombination dynamics,” J. Am. Chem. Soc.  131, 9020–9025 (2009).  Link

  72. H. Peter Lu, "Single-Molecule Protein Interaction Conformational Dynamics," Current Pharmaceutical Biotechnology, 10, 522-531 (2009). Link

  73. H. Peter Lu, "Combined Single-Molecule Electrical Recording and Single-Molecule Spectroscopy Studies of Ion Channel Conformational Dynamics," an invited book chapter in Methods in Nano Cell Biology, edited by Bhanu Jena, ELSEVIER (2009).

  74. Yuanmin Wang, Xuefei Wang, Sujit Kumar Ghosh, H. Peter Lu, "Probing single-molecule interfacial electron transfer dynamics of porphyrin on TiO2 nanoparticles," J. Am. Chem. Soc. 131, 1479-1487 (2009). Link

  75. Xuefei Wang, and H. Peter Lu, "2D Regional Correlation Analysis of Single-Molecule Time Trajectories,"  J. Phys. Chem. B. 112, 14920-14926 (2008). Link

  76. Duohai Pan, Dehong Hu, Ruchuan Liu, Xiaohua Zeng, Samuel Kaplan, H. Peter Lu, “Fluctuating Two-State Light Harvesting in a Photosynthetic Membrane,” J. Phys. Chem. C, 111, 8948-8956 (2007). Link

  77. Qiang Lu, H. Peter Lu, and Jin Wang, “Exploring the Mechanism of Flexible Biomolecular Recognition with Single Molecule Dynamics,” Phys. Rev. Lett. 98, 128105 (2007). Link

  78. V. Biju, D. Pan, Yuri A. Gorby, Jim Fredrickson, J. Mclean, D. Saffarini and H. Peter Lu , "Correlated Spectroscopic and Topographic Characterization of Nanoscale Domains and Their Distributions of a Redox Protein on Bacterial Cell Surfaces," Langmuir 23, 1333-1338 (2007). Link

  79. Ruchuan Liu, Dehong Hu, Xin Tan, and H. Peter Lu, "Revealing Two-State Protein-Protein Interactions of Calmodulin by Single-Molecule Spectroscopy," J. Am. Chem. Soc. 128, 10034-10042 (2006). Link

  80. Jin Wang, Qiang Lu, and H. Peter Lu, "Single-Molecule Dynamics Reveals Cooperative Binding-Folding in Protein Recognition," PLoS Computational Biology, 2, 842-852 (2006). Link

  81. Dehong Hu and H. Peter Lu, "Single molecule electron transfer process of ruthenium complexes," Proc. SPIE Vol. 6092, 609207 (2006). 

  82. T. Zhang, S. N. Danthi, J. Xie, D. Hu, H. P. Lu, and K. Li, "Live cell imaging of the endocytosis and the intracellular trafficking of multifunctional lipid nanoparticles," Proc. SPIE Vol. 6095, 60950D (2006). 

  83. Duohai Pan, Nick Klymyshyn, Dehong Hu, and H. Peter Lu, "Tip-enhanced near-field Raman spectroscopy probing single dye-sensitized TiO2 nanoparticles," Appl. Phys. Lett., 88, 093121(2006). Link

  84. Duohai Pan, Dehong Hu, and H. Peter Lu, "Probing Inhomogeneous Vibrational Reorganization Energy Barriers of Interfacial Electron Transfer," J. Phys. Chem. B, 109, 16390-16395 (2005) (Cover page). Link

  85. Dehong Hu and H. Peter Lu, "Single-Molecule Triplet-State Photon Antibunching at Room Temperature," J. Phys. Chem. B, 109, 9861-9864 (2005). Link

  86. H. Peter Lu, invited review article, "Probing Single-Molecule Protein Conformational Dynamics," Acc. Chem. Res. 38, 557-565 (2005). Link

  87. H. Peter Lu, "Single-Molecule Study of Protein-Protein and Protein-DNA Interaction Dynamics," an invited book chapter in Protein-Ligand Interactions, edited by Uli Nienhaus, The Humana Press Inc., 2005. 

  88. H. Peter Lu, invited review article, "Site-Specific Raman Spectroscopy and Chemical Dynamics of Nanoscale Interstitial Systems," J. Physics: Condensed Matter, 17, R333-R355 (2005).Link

  89. V. Biju, Miodrag Micic, Dehong Hu, and H. Peter Lu, "Intermittent Single-Molecule Interfacial Electron Transfer Dynamics," J. Am. Chem. Soc. 126, 9374-9381 (2004). Link

  90. Xin Tan, Dehong Hu, Thomas C. Squier, and H. Peter Lu, "Probing Nanosecond Protein Motions of Calmodulin by Single-Molecule Fluorescence Anisotropy," Applied Phys. Lett., 85, 2420-2422 (2004).  Link

  91. Miodrag Micic, Dehong Hu, Greg Newton, Margie Romine, H. Peter Lu, "Correlated Atomic Force Microscopy and Fluorescence Lifetime Imaging of Live Bacterial Cells," Surface and Colloid B, 34, 205-212 (2004). Link

  92. H. Peter Lu, invited review, "Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions," a special issue of Curr Pharm Biotech (The way down from single genes, and proteins to single molecules.), 5, 261-269 (2004). Link

  93. Dehong Hu, H. Peter Lu, "Single Molecule Implanting of T4 Lysozyme on Bacterial Cell Surface: Towards Study Single Molecule Enzymatic Reaction in Living Cells," Biophys. J., 87, 656-661 (2004). Link

  94. D. Hu, M. Micic, N. Klymyshyn, Y. D. Suh, H. Peter Lu, "Correlated topographic and spectroscopic imaging by combined atomic force microscopy and optical microscopy," J. Luminescence, 107, 4-12 (2004). Link

  95. G. Harms, G. Orr, H. Peter Lu, "Probing ion channel conformational dynamics using simultaneous single-molecule ultrafast spectroscopy and patch-clamp electric recording," Appl. Phys. Lett., 84, 1792-1794 (2004). Link

  96. Xin Tan, Perihan Nalbant, Alexei Toutchkine, Dehong Hu, Erich R. Vorpagel, Klaus M. Hahn, and H Peter Lu, "Single-Molecule Study of Protein-Protein Interaction Dynamics in a Cell Signaling System," J. Phys. Chem. B., 108, 737 (2004). Link

  97. Miodrag Micic, Nicholas Klymyshyn, H. Peter Lu, "Finite Element Method Simulations of the Near-Field Enhancement at the vicinity of Fractal Rough Metallic Surfaces," J. Phys. Chem. B., 108, 2939 (2004). Link

  98. Dehong Hu, Miodrag Micic, Nicholas Klymyshyn, Yung Doug Suh, and H. Peter Lu "Correlated Topographic and Spectroscopic Imaging Beyond Diffraction Limit by Atomic Force Microscopy Metallic Tip-Enhanced Near-Field Fluorescence Lifetime Microscopy," Rev. Sci. Inst., 74, 3347 (2003). Link

  99. Yu Chen, Dehong Hu, Erich R. Vorpagel, and H. Peter Lu, "Probing Single-Molecule T4 Lysozyme Conformational Dynamics by Intramolecular Fluorescence Energy Transfer," J. Phys. Chem. B, 107, 7947 (2003). Link

  100. Greg S. Harms, Galya Orr, Mauricio Montal, Brian D. Thrall, Steve D. Colson, H. Peter Lu, "Probing Conformational Changes of Gramicidin Ion Channels by Single-Molecule Patch-Clamp Fluorescence Microscopy," Biophys. J., 85, 1826 (2003). Link

  101. Dehong Hu and H. Peter Lu, "Single-Molecule Nanosecond Anisotropy Dynamics of Tethered Protein Motions," J. Phys. Chem. B, 107, 618 (2003) (Cover page). Link

Updated: 09/02/2022 10:38AM