English
Related papers

Related papers: Two-state folding over a weak free-energy barrier

200 papers

The determination of the folding mechanisms of proteins is critical to understand the topological change that can propagate Alzheimer and Creutzfeld-Jakobs diseases, among others. The computational community has paid considerable attention…

Biomolecules · Quantitative Biology 2007-05-23 Guanghong Wei , Normand Mousseau , Philippe Derreumaux

The Metropolis Monte Carlo (MC) method is used to extract reaction kinetics from a given equilibrium distribution of states of a complex system. The approach is illustrated by the folding/unfolding reaction for two proteins - a model…

Biological Physics · Physics 2022-03-23 Sergei F. Chekmarev

We demonstrate that the recently proposed pruned-enriched Rosenbluth method PERM (P. Grassberger, Phys. Rev. E, in press (1997)) leads to extremely efficient algorithms for the folding of simple model proteins. We test it on several models…

Statistical Mechanics · Physics 2007-05-23 Ugo Bastolla , Helge Frauenkron , Erwin Gerstner , Peter Grassberger , Walter Nadler

We test a simplified, local version of the helix model on two synthetic and two natural proteins, to study its efficiency in predicting the native secondary structure. The results we obtain are very good for the synthetic sequences, poorer…

Soft Condensed Matter · Physics 2009-10-30 Pierpaolo Bruscolini

The concept of a protein diffusing in its free energy folding landscape has been fruitful for both theory and experiment. Yet the choice of the reaction coordinate (RC) introduces an undesirable degree of arbitrariness into the problem. We…

Biological Physics · Physics 2015-05-19 Michael Hinczewski , Yann von Hansen , Joachim Dzubiella , Roland R. Netz

We demonstrate that the recently proposed pruned-enriched Rosenbluth method PERM (P.~Grassberger, Phys.~Rev.~{\bf E 56} (1997) 3682) leads to very efficient algorithms for the folding of simple model proteins. We test it on several models…

Soft Condensed Matter · Physics 2007-05-23 H. Frauenkron , U. Bastolla , E. Gerstner , P. Grassberger , und W. Nadler

ZSPA-1 is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed ZSPA-1 shows a reduced helix content and a melting behavior that is less cooperative, compared with the…

Biomolecules · Quantitative Biology 2007-05-23 Giorgio Favrin , Anders Irbäck , Stefan Wallin

The processes by which protein sidechains reach equilibrium during a folding reaction are investigated using both lattice and all-atom simulations. We find that rates of sidechain relaxation exhibit a distribution over the protein…

Soft Condensed Matter · Physics 2007-05-23 E. Kussell , J. Shimada , E. I. Shakhnovich

Current theories of heteropolymers are inherently macrpscopic, but are applied to folding proteins which are only mesoscopic. In these theories, one computes the averaged free energy over sequences, always assuming that it is self-averaging…

Soft Condensed Matter · Physics 2009-11-07 Jeffrey Chuang , Alexander Yu. Grosberg , Mehran Kardar

In spite of decades of research, much remains to be discovered about folding: the detailed structure of the initial (unfolded) state, vestigial folding instructions remaining only in the unfolded state, the interaction of the molecule with…

Biological Physics · Physics 2018-11-26 Walter A. Simmons

Exploring and understanding the protein-folding problem has been a long-standing challenge in molecular biology. Here, using molecular dynamics simulation, we reveal how parallel distributed adjacent planar peptide groups of unfolded…

Biomolecules · Quantitative Biology 2019-01-11 Xiaoliang Ma , Chengyu Hou , Liping Shi , Long Li , Jiacheng Li , Lin Ye , Lin Yang , Xiaodong He

Natural protein sequences that self-assemble to form globular structures are compact with high packing densities in the folded states. It is known that proteins unfold upon addition of denaturants, adopting random coil structures. The…

Biomolecules · Quantitative Biology 2016-12-02 Himadri S. Samanta , Pavel I. Zhuravlev , Michael Hinczewski , Naoto Hori , Shaon Chakrabarti , D. Thirumalai

We study folding dynamics of protein-like sequences on square lattice using physical move set that exhausts all possible conformational changes. By analytically solving the master equation, we follow the time-dependent probabilities of…

Biomolecules · Quantitative Biology 2016-08-16 Sëma Kachalo , Hsiao-Mei Lu , Jie Liang

The importance of torsion vibration in the transmission of life information is indicated. The localization of quantum torsion state is proved. Following these analyses a formalism on the quantum theory of conformation-electron system is…

Biomolecules · Quantitative Biology 2009-06-16 Liaofu Luo

The coil to globule transition of the polypeptide chain is the physical phenomenon behind the folding of globular proteins. Globular proteins with a single domain usually consist of about 30 to 100 amino acid residues, and this finite size…

Biomolecules · Quantitative Biology 2020-10-27 Artem Badasyan , Matjaz Valant , Joze Grdadolnik , Vladimir N. Uversky

We report a computer simulation study of a model gel-former obtained by modifying the three-body interactions of the Stillinger-Weber potential for silicon. This modification reduces the average coordination number and consequently shifts…

Disordered Systems and Neural Networks · Physics 2015-05-27 Shibu Saw , Niels L. Ellegaard , Walter Kob , Srikanth Sastry

Using a structure-based coarse-grained model of proteins, we study the mechanism of unfolding of knotted proteins through heating. We find that the dominant mechanisms of unfolding depend on the temperature applied and are generally…

Biomolecules · Quantitative Biology 2017-01-23 Yani Zhao , Mateusz Chwastyk , Marek Cieplak

Mechanical stretching of six proteins is studied through molecular dynamics simulations. The model is Go-like, with Lennard-Jones interactions at native contacts. Low temperature unfolding scenarios are remarkably complex and sensitive to…

Biomolecules · Quantitative Biology 2009-11-10 Marek Cieplak , Trinh Xuan Hoang , Mark O. Robbins

Understanding the mechanism of protein secondary structure formation is an essential part of protein-folding puzzle. Here we describe a simple model for the formation of the $\beta$-hairpin, motivated by the fact that folding of a…

Soft Condensed Matter · Physics 2009-10-31 Chinlin Guo , Herbert Levine , David Kessler

The aqueous solvent profoundly influences protein folding, yet its effects are relatively poorly understood. In this study, we investigate the impact of solvation on the folding of lattice proteins by using Monte Carlo simulations. The…

Soft Condensed Matter · Physics 2025-04-01 Nhung T. T. Nguyen , Pham Nam Phong , Duy Manh Le , Minh-Tien Tran , Trinh Xuan Hoang