Volk, Martin - University of Liverpool - Department of Chemistry

个人简介

Dr. Volk’s research interests focus on the application of time-resolved spectroscopy to the investigation of a broad range of chemical and biological processes. These include the dissociation and coherent motion of small molecules, inter- and intramolecular electron transfer in model systems and proteins, and ligand dynamics and energy relaxation in heme proteins. In Liverpool, Dr. Volk started to investigate fast processes of protein folding, using a nanosecond temperature-jump setup with high signal-to-noise IR detection. With this highly sensitive setup, he made major world-recognised contributions to the current knowledge of fast protein folding dynamics, especially of alpha-helix folding dynamics. More recently, he became involved in research on gold nanoparticles, esp. the structure and dissociation dynamics of peptide capping layers on such nanoparticles and the application of gold nanoparticles in photodynamic therapy. Invited Talk "Probing the Ligand Shell of Nanoparticles: Opportunities and Limitations" (Invitation to Speak, NPL Focus User Meeting on Differential Centrifugal Sedimentation 2016) Invited talk "Characterising Protein and Peptide Layers on Gold Nanoparticles" (Invitation to Speak, ACS Annual Meeting 2015) Invited seminar "Laser-induced Delivery and Release of Biomolecules into Cells Using Gold Nanop..." (Invitation to Speak, Ecole Polytechnique, Palaiseau, France 2010) Invited seminar "Laser-induced Delivery and Release of Biomolecules into Cells Using Gold Nanopa..." (Invitation to Speak, Bionano seminar series University of Liverpool 2010) Invited seminar "Temperature Jumps for Studying Protein/Peptide Folding" (Invitation to Speak, Bionano seminar series University of Liverpool 2010) Invited talk "Laser-induced Delivery and Release of Biomolecules into Cells Using Gold Nanoparticles (Invitation to Speak, STFC 2010) Invited seminar "Fast Processes of Alpha-Helix Folding" (Invitation to Speak, Ecole Polytechnique, Palaiseau, France 2008) Invited talk "Correlation Between Side Chain Helix Propensity and Fast Folding Dynamics of..." (Invitation to Speak, ACS 2007) Invited talk "Fast Processes of Alpha-Helix Folding" (Invitation to Speak, CCLRC 2007) Invited seminar "Fast Processes of Alpha-Helix Folding" (Invitation to Speak, University of Leeds 2007) Invited talk "Correlation between Side Chain Helix Propensity and Fast Folding Dynamics..." (Invitation to Speak, Biophysical Society 2006) Invited talk "Correlation Between Side Chain Helix Propensities and Fast Folding Dynamics..." (Invitation to Speak, CCLRC 2006) Invited seminar "Fast Processes of Alpha-Helix Folding" (Invitation to Speak, Mount Holyoke College, South Hadley, USA 2006) Invitation to chair platform session (Biophysical Society 2006) Invited talk "Time-resolved isotope-edited IR spectroscopy reveals details of fast peptide folding.. (Invitation to Speak, IRDG 2006) Invitation to contribute to special issue in Chemical Physics (Chemical Physics editorial board 2005) Invited seminar "Fast Folding Dynamics of Alpha-Helical Peptides" (Invitation to Speak, Swarthmore College, Swarthmore USA 2004) Invited talk "Time-Resolved Isotope-Edited Infrared Spectroscopy" (Invitation to Speak, CCLRC 2004) Invited seminar "Fast Folding Dynamics of Alpha-Helical Peptides" (Invitation to Speak, University of Leeds 2003) Invited Microreview in the European Journal of Organic Chemistry (European Journal of Organic Chemistry 2001) Invited seminar "Rotational and Librational Motion of Dissociation Products on the fs-Timescale" (Invitation to Speak, University of Birmingham 2001)

研究领域

Dr. Volk’s research interests focus on the application of time-resolved spectroscopy to the investigation of a broad range of chemical and biological processes. These include the dissociation and coherent motion of small molecules, inter- and intramolecular electron transfer in model systems and proteins, and ligand dynamics and energy relaxation in heme proteins. In Liverpool, Dr. Volk started to investigate fast processes of protein folding, using a nanosecond temperature-jump setup with high signal-to-noise IR detection. With this highly sensitive setup, he made major world-recognised contributions to the current knowledge of fast protein folding dynamics, especially of alpha-helix folding dynamics. More recently, he became involved in research on gold nanoparticles, esp. the structure and dissociation dynamics of peptide capping layers on such nanoparticles and the application of gold nanoparticles in photodynamic therapy.

近期论文

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Characterizing Self-Assembled Monolayers on Gold Nanoparticles Computational and Experimental Investigation of the Structure of Peptide Monolayers on Gold Nanoparticles Singlet Oxygen Generation by Laser Irradiation of Gold Nanoparticles Stabilization of Insulin by Adsorption on a Hydrophobic Silane Self-Assembled Monolayer The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone High-Resolution Sizing of Monolayer-Protected Gold Clusters by Differential Centrifugal Sedimentation pH-dependent helix folding dynamics of poly-glutamic acid Amyloid-Derived Peptide Forms Self-Assembled Monolayers on Gold Nanoparticle with a Curvature-Dependent β-Sheet Structure Measurement of energy landscape roughness of folded and unfolded proteins The intracellular Ig fold: a robust protein scaffold for the engineering of molecular recognition Measurement of circular dichroism dynamics in a nanosecond temperature-jump experiment Inflicting Controlled Nonthermal Damage to Subcellular Structures by Laser-Activated Gold Nanoparticles Laser-induced Delivery of Gold Nanoparticles into Living Cells Polymer Coil-Globule Transition Dynamics on the Nanosecond Time Scale Nitrobenzyl Phototrigger for Fast Protein Folding Processes Synthesis of Co Nanoparticles by Pulsed Laser Irradiation of Cobalt Carbonyl in Organic Solution Universal scaling law for polypeptide backbone dynamics on the pico- to millisecond time scale Using atomic force microscopy to measure mechanical strength of nanometre scale protein fibrils UV Resonance Raman Spectroscopy reveals details of the 'Random Coil' State of Polypeptides Correlation between side chain helix propensity and fast folding dynamics of a-helical peptides Fast folding dynamics of α-helical peptides – Effect of solvent additives and pH Optical Spectroscopy in Chemistry and Life Sciences (by Werner Schmidt) The effect of solvent additives and pH on the fast folding dynamics of alanine-based a-helical model peptides Time-resolved isotope-edited infrared spectroscopy reveals that the a-helix folds more rapidly at the C-terminus than at the N-terminus The effects of individual amino acids on the fast folding dynamics of α-helical peptides