English
Related papers

Related papers: Flexibility of beta-sheets: Principal-component an…

200 papers

In simple models side chains are often represented implicitly (e.g., by spin-states) or simplified as one atom. We study side chain effects using square lattice and tetrahedral lattice models, with explicitly side chains of two atoms. We…

Biomolecules · Quantitative Biology 2009-11-10 Jinfeng Zhang , Yu Chen , Rong Chen , Jie Liang

The intricate three-dimensional geometries of protein tertiary structures underlie protein function and emerge through a folding process from one-dimensional chains of amino acids. The exact spatial sequence and configuration of amino…

Biomolecules · Quantitative Biology 2021-02-24 Nora Molkenthin , Steffen Mühle , Antonia S J S Mey , Marc Timme

Principal components (PCA) and hierarchical clustering are two of the most heavily used techniques for analyzing the differences between nucleic acid sequence samples sampled from a given environment. However, a classical application of…

Populations and Evolution · Quantitative Biology 2011-07-27 Frederick A. Matsen , Steven N. Evans

Protein-nucleic acid complexes are important for many cellular processes including the most essential function such as transcription and translation. For many protein-nucleic acid complexes, flexibility of both macromolecules has been shown…

Biomolecules · Quantitative Biology 2015-10-28 Kristopher Opron , Kelin Xia , Zachary F. Burton , Guo-Wei Wei

Lattice-model simulations and experiments of some small proteins suggest that folding is essentially controlled by a few conserved contacts. Residues of these conserved contacts form the minimum set of native contacts needed to ensure…

Biomolecules · Quantitative Biology 2011-09-14 Wei-Mou Zheng , Hui Zeng , Dong-Bo Bu , Ming-Fu Shao , Ke-Song Liu , Chao Wang

The protein folding problem has attracted an increasing attention from physicists. The problem has a flavor of statistical mechanics, but possesses the most common feature of most biological problems -- the profound effects of evolution. I…

Statistical Mechanics · Physics 2009-10-31 Chao Tang

Woven shell structures are beneficial for applications requiring lightweight, damage resilience, and design tunability, such as in wearable devices, soft robotics, and aerospace systems. A fundamental component of woven structures is the…

Applied Physics · Physics 2025-12-02 Jaimie Krankel , Guowei Wayne Tu , Evgueni T. Filipov

This study examines the mechanical behavior of a novel class of mechanical metamaterials alternating pentamode lattices and stiffening plates. The unit cell of such lattices consists of a sub-lattice of the face cubic-centered unit cell…

Applied Physics · Physics 2020-02-04 F. Fraternali , A. Amendola

Soft gels, formed via the self-assembly of particulate organic materials, exhibit intricate multi-scale structures that provides them with flexibility and resilience when subjected to external stresses. This work combines molecular…

Soft Condensed Matter · Physics 2024-04-05 Alexander Smith , Gavin J. Donley , Emanuela Del Gado , Victor M. Zavala

Elastic network models (ENM) and constraint-based, topological rigidity analysis are two distinct, coarse-grained approaches to study conformational flexibility of macromolecules. In the two decades since their introduction, both have…

Biomolecules · Quantitative Biology 2018-02-27 Dominik Budday , Sigrid Leyendecker , Henry van den Bedem

We consider six different secondary structures of proteins and construct two types of Go-type off-lattice models: with the steric constraints and without. The basic aminoacid-aminoacid potential is Lennard Jones for the native contacts and…

Statistical Mechanics · Physics 2009-10-31 Trinh Xuan Hoang , Marek Cieplak

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

Methods from artificial intelligence (AI), in general, and machine learning, in particular, have kept conquering new territories in numerous areas of science. Most of the applications of these techniques are restricted to the classification…

Biomolecules · Quantitative Biology 2022-10-24 Kristof Takacs , Balint Varga , Viktor Farkas , Andras Perczel , Vince Grolmusz

Protein folding cooperativity is defined by the nature of the finite-size thermodynamic transition exhibited upon folding: two-state transitions show a free energy barrier between the folded and unfolded ensembles, while downhill folding is…

Biomolecules · Quantitative Biology 2017-08-23 Tristan Bereau , Michael Bachmann , Markus Deserno

A simplified interaction potential for protein folding studies at the atomic level is discussed and tested on a set of peptides with about 20 residues each. The test set contains both alpha-helical (Trp cage, Fs) and beta-sheet (GB1p,…

Biomolecules · Quantitative Biology 2009-11-10 Anders Irbäck , Sandipan Mohanty

The principal component analysis (PCA), a mathematical tool commonly used in statistics, has recently been employed to interpret the $p_T$-dependent fluctuations of harmonic flow $v_n$ in terms of leading and subleading flow modes in heavy…

Nuclear Experiment · Physics 2020-08-26 Ziming Liu , Arabinda Behera , Huichao Song , Jiangyong Jia

While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learned how to extract this information to predict the three--dimensional, biologically active, native conformation of…

Biomolecules · Quantitative Biology 2009-11-10 R. A. Broglia , G. Tiana

The determination of a 'folding core' can help to provide insight into the structure, flexibility, mobility and dynamics, and hence, ultimately, function of a protein - a central concern of structural biology. Changes in the folding core…

Biomolecules · Quantitative Biology 2015-04-09 J. W. Heal , R. A. Römer , C. A. Blindauer , R. B. Freedman

Neither of the two prevalent theories, namely thermodynamic stability and kinetic stability, provides a comprehensive understanding of protein folding. The thermodynamic theory is misleading because it assumes that free energy is the…

Biological Physics · Physics 2013-07-22 Ji Xu , Mengzhi Han , Ying Ren , Jinghai Li

We discuss recent theoretical developments in the study of simple lattice models of proteins. Such models are designed to understand general features of protein structures and mechanism of folding. Among the topics covered are (i) the use…

Soft Condensed Matter · Physics 2007-05-23 D. Thirumalai , D. K. Klimov