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Dynamics of Proteins

Berichte der Bunsengesellschaft für physikalische Chemie, 1982
Theoretical methods for studying protein motions have been outlined and some examples have been given. Simulation methods have shown that structural fluctuations in proteins cover a wide range in their magnitudes and time scales. Some indication of their biological role has been given, but the most important and interesting applications to protein ...
P G Debrunner, H Frauenfelder
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Essential dynamics of proteins

Proteins: Structure, Function, and Bioinformatics, 1993
AbstractAnalysis of extended molecular dynamics (MD) simulations of lysozyme in vacuo and in aqueous solution reveals that it is possible to separate the configurational space into two subspaces: (1) an “essential” subspace containing only a few degrees of freedom in which anharmonic motion occurs that comprises most of the positional fluctuations; and
AMADEI, A, LINSSEN, ABM, BERENDSEN, HJC
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Chaos in protein dynamics

Proteins: Structure, Function, and Genetics, 1997
MD simulations, currently the most detailed description of the dynamic evolution of proteins, are based on the repeated solution of a set of differential equations implementing Newton's second law. Many such systems are known to exhibit chaotic behavior, i.e., very small changes in initial conditions are amplified exponentially and lead to vastly ...
M, Braxenthaler   +4 more
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LARMD: integration of bioinformatic resources to profile ligand-driven protein dynamics with a case on the activation of estrogen receptor

Briefings Bioinform., 2019
Protein dynamics is central to all biological processes, including signal transduction, cellular regulation and biological catalysis. Among them, in-depth exploration of ligand-driven protein dynamics contributes to an optimal understanding of protein ...
Jing-Fang Yang   +4 more
semanticscholar   +1 more source

Protein Dynamism and Evolvability

Science, 2009
The traditional view that proteins possess absolute functional specificity and a single, fixed structure conflicts with their marked ability to adapt and evolve new functions and structures. We consider an alternative, “avant-garde view” in which proteins are conformationally dynamic and exhibit functional promiscuity.
Nobuhiko, Tokuriki, Dan S, Tawfik
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Protein-folding dynamics

Nature, 1976
In a discussion of the dynamics of protein folding two limiting models (random-search nucleation and chain propagation., diffusion–collision) are considered. It is suggested that the latter may have the dominant role in many proteins.
M, Karplus, D L, Weaver
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Integration of network models and evolutionary analysis into high-throughput modeling of protein dynamics and allosteric regulation: theory, tools and applications

Briefings Bioinform., 2019
Proteins are dynamical entities that undergo a plethora of conformational changes, accomplishing their biological functions. Molecular dynamics simulation and normal mode analysis methods have become the gold standard for studying protein dynamics ...
Zhong-Jie Liang   +2 more
semanticscholar   +1 more source

Dynamics of folded proteins

Nature, 1977
The dynamics of a folded globular protein (bovine pancreatic trypsin inhibitor) have been studied by solving the equations of motion for the atoms with an empirical potential energy function. The results provide the magnitude, correlations and decay of fluctuations about the average structure.
J A, McCammon, B R, Gelin, M, Karplus
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Protein dynamics and conformational changes explored by hydrogen/deuterium exchange mass spectrometry.

Current Opinion in Structural Biology, 2019
Proteins are not rigid bodies under their physiological conditions. Here we discuss a solution-phase structural proteomics technique, hydrogen deuterium exchange coupled with mass spectrometry (HDX-MS), as a means to study protein dynamics, which can ...
Jie Zheng   +3 more
semanticscholar   +1 more source

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