NIH VideoCast - Molecular simulation tools for investigating structure and dynamics of intrinsically disordered proteins

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Molecular simulation tools for investigating structure and dynamics of intrinsically disordered proteins

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Air date:	Friday, June 1, 2018, 12:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 109 (33 Live, 76 On-demand)
Category:	NIH Director's Seminars
Runtime:	00:54:21
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	Director's Seminar Series Dr. Robert Best's research is concerned with the dynamics of large biomolecules and in particular with protein dynamics, folding, and misfolding. Novel simulation and theoretical methods are developed as needed to address specific problems. A strong emphasis is placed on making a connection with experiment, both in using experimental data to help improve simulation methodology or sampling, and simulations as a tool to assist the interpretation of results. Recent work has focused on the following: The optimization of protein force fields using empirical data for peptides and macromolecules in solution; interpretation of single-molecule fluorescence or pulling experiments using simulation and theory; coarse-grained master equations as a tool for interpreting peptide dynamics in simulations; diffusion models of protein folding; the binding mechanism of intrinsically disordered proteins; the influence of molecular chaperonins on folding and misfolding; the mechanism of substrate transport in hydrogenase enzymes; and methods for identifying cryptic binding pockets in proteins.

NLM Title:	Molecular simulation tools for investigating structure and dynamics of intrinsically disordered proteins / Robert Best.
Author:	Best, Robert. National Institutes of Health (U.S.),
Publisher:
Abstract:	(CIT): Director's Seminar Series Dr. Robert Best's research is concerned with the dynamics of large biomolecules and in particular with protein dynamics, folding, and misfolding. Novel simulation and theoretical methods are developed as needed to address specific problems. A strong emphasis is placed on making a connection with experiment, both in using experimental data to help improve simulation methodology or sampling, and simulations as a tool to assist the interpretation of results. Recent work has focused on the following: The optimization of protein force fields using empirical data for peptides and macromolecules in solution; interpretation of single-molecule fluorescence or pulling experiments using simulation and theory; coarse-grained master equations as a tool for interpreting peptide dynamics in simulations; diffusion models of protein folding; the binding mechanism of intrinsically disordered proteins; the influence of molecular chaperonins on folding and misfolding; the mechanism of substrate transport in hydrogenase enzymes; and methods for identifying cryptic binding pockets in proteins.
Subjects:	Fluorescence Resonance Energy Transfer Intrinsically Disordered Proteins--analysis Molecular Dynamics Simulation Protein Conformation Protein Folding
Publication Types:	Lecture Webcast

NLM Classification:	QU 55
NLM ID:	101729815
CIT Live ID:	27907
Permanent link:	https://videocast.nih.gov/watch=27907

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