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Related papers: The Role of Structure in the Protein Dynamical Tra…

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To characterize the thermodynamical equilibrium of DNA chains interacting with a solution of non-specific binding proteins, a Flory-Huggins free energy model was implemented. We explored the dependence on DNA and protein concentrations of…

Soft Condensed Matter · Physics 2015-11-04 Guillaume Le Treut , François Képès , Henri Orland

The dynamics of lysozyme is probed by attaching -SCN to all alanine-residues. The 1-dimensional infrared spectra exhibit frequency shifts in the position of the maximum absorption by 4 cm$^{-1}$ which is consistent with experiments in…

Chemical Physics · Physics 2024-04-30 Sena Aydin , Seyedeh Maryam Salehi , Kai Töpfer , Markus Meuwly

The Langevin dynamics of a random heteropolymer and its dynamic glass transition are studied using elementary mode coupling theory. Contrary to recent reports using a similar framework, a discontinuous ergodic-nonergodic phase transition is…

Statistical Mechanics · Physics 2009-10-30 Shoji Takada , John J. Portman , Peter G. Wolynes

Conformational changes upon protein-protein association are the key element of the binding mechanism. The study presents a systematic large-scale analysis of such conformational changes in the side chains. The results indicate that short…

Biomolecules · Quantitative Biology 2010-10-15 Anatoly M. Ruvinsky , Tatsiana Kirys , Alexander V. Tuzikov , Ilya A. Vakser

An important question in molecular evolution is whether an amino acid that occurs at a given position makes an independent contribution to fitness, or whether its effect depends on the state of other loci in the organism's genome, a…

Populations and Evolution · Quantitative Biology 2013-09-05 David M. McCandlish , Etienne Rajon , Premal Shah , Yang Ding , Joshua B. Plotkin

Statistical thermodynamics basis of energy and residue position fluctuations is explained for native proteins. The protein and its surroundings are treated as a canonical system with emphasis on the effects of energy exchange between the…

Biological Physics · Physics 2015-05-28 Burak Erman

The low-frequency collective vibrational modes in proteins as well as the protein-water interface have been suggested as dominant factors controlling the efficiency of biochemical reactions and biological energy transport. It is thus…

Biological Physics · Physics 2019-03-29 Ali Charkhesht , Chola K. Regmi , Katie R. Mitchell-Koch , Shengfeng Cheng , Nguyen Q. Vinh

Functional proteins must fold with some minimal stability to a structure that can perform a biochemical task. Here we use a simple model to investigate the relationship between the stability requirement and the capacity of a protein to…

Biomolecules · Quantitative Biology 2009-11-10 Jesse D Bloom , Claus O Wilke , Frances H Arnold , Christoph Adami

We study the combined influence of amino acid composition and chain length on the thermal stability of protein structures. A new parameterization of the internal free energy is considered, as the sum of hydrophobic effect, hydrogen-bond and…

Genomics · Quantitative Biology 2012-05-07 Antonio Deiana , Kana Shimizu , Andrea Giansanti

Proteins have evolved through mutations, amino acid substitutions, since life appeared on Earth, some 109 years ago. The study of these phenomena has been of particular significance because of their impact on protein stability, function,…

Biomolecules · Quantitative Biology 2023-10-25 Jorge A. Vila

What are the molecular mechanisms that dictate protein-protein binding stability and whether those are related to the ones behind protein fold stability are still largely open questions. Indeed, despite many past efforts, we still lack…

Biological Physics · Physics 2023-11-28 Fausta Desantis , Mattia Miotto , Lorenzo Di Rienzo , Edoardo Milanetti , Giancarlo Ruocco

In order to inquire the microscopic origin of observed multiple time scales in solvation dynamics we carry out several computer experiments. We perform atomistic molecular dynamics simulations on three protein-water systems namely,…

Soft Condensed Matter · Physics 2017-10-18 Sayantan Mondal , Saumyak Mukherjee , Biman Bagchi

The theory of biochemical processes needs simple but realistic models of phenomena underlying microscopic dynamics of proteins. Many experiments performed in the 1980s have demonstrated that within the protein native state, apart from usual…

Condensed Matter · Physics 2007-05-23 Michal Kurzynski

The growing interest for comparing protein internal dynamics owes much to the realization that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional…

Biomolecules · Quantitative Biology 2012-12-19 C. Micheletti

A central goal of protein-folding theory is to predict the stochastic dynamics of transition paths --- the rare trajectories that transit between the folded and unfolded ensembles --- using only thermodynamic information, such as a…

Biomolecules · Quantitative Biology 2018-08-09 William M. Jacobs , Eugene I. Shakhnovich

We study the thermodynamic behavior of a simple off-lattice model for protein folding. The model is two-dimensional and has two different ``amino acids''. Using numerical simulations of all chains containing eight or ten monomers, we…

chem-ph · Physics 2009-10-28 Anders Irbäck , Frank Potthast

We discuss general thermodynamic properties of molecular structure formation processes like protein folding by means of simplified, coarse-grained models. The conformational transitions accompanying these processes exhibit similarities to…

Soft Condensed Matter · Physics 2011-07-04 Michael Bachmann

A phase transition indicates a sudden change in the properties of a large system. For temperature-driven phase transitions this is related to non-analytic behavior of the free energy density at the critical temperature: The knowledge of the…

Statistical Mechanics · Physics 2015-03-20 Markus Heyl , Anatoli Polkovnikov , Stefan Kehrein

PDZ (Post-synaptic density-95/discs large/zonula occludens-1) domains are relatively small (80 to 120 residues) protein binding modules central in the organization of receptor clusters and in the association of cellular proteins. Their main…

In this work we study, at the single molecular level, the thermodynamic and dynamic characteristics of an enzymatic reaction comprising a rate limiting step. We investigate how the stability of the enzyme-state stationary probability…

Subcellular Processes · Quantitative Biology 2015-05-20 Moisés Santillán
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