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A protein structure is represented as a network of residues whereby edges are determined by intra-molecular contacts. We introduce inhomogeneity into these networks by assigning each edge a weight that is determined by amino-acid pair…

Soft Condensed Matter · Physics 2007-06-13 Ali Rana Atilgan , Deniz Turgut , Canan Atilgan

Large language models from different families use different hidden dimensions, tokenizers, and training procedures, making behavioral directions difficult to compare or transfer across models. We introduce an anchor-projection framework…

Artificial Intelligence · Computer Science 2026-05-12 Su-Hyeon Kim , Yo-Sub Han

Over the last years, analyses performed on a stochastic model of catalytic reaction networks have provided some indications about the reasons why wet-lab experiments hardly ever comply with the phase transition typically predicted by…

Computational Engineering, Finance, and Science · Computer Science 2013-10-01 Chiara Damiani , Alessandro Filisetti , Alex Graudenzi , Marco Villani , Roberto Serra

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

This paper reports about an approach to the classification of proteins' primary structures taking advantage of the Self Organizing Maps algorithm and of a numerical coding of the aminoacids based upon their physico-chemical properties.…

Biological Physics · Physics 2007-05-23 P. Sirabella , A. Giuliani , A. Colosimo

An In Silico model to relate the properties of proteins to the structure, sequence, function and evolutionary history of proteins is shown. The derived ideal sequences for amino acid residues in proteins can then be considered as attractors…

Condensed Matter · Physics 2007-05-23 S. Bumble

Understanding the link between structure and function in proteins is fundamental in molecular biology and proteomics. A central question in this context is whether allostery - where the binding of a molecule at one site affects the activity…

Statistical Mechanics · Physics 2025-06-02 Giulio Costantini , Lorenzo Caprini , Umberto Marini Bettolo Marconi , Fabio Cecconi

Allosteric regulation at distant sites is central to many cellular processes. In particular, allosteric sites in proteins are a major target to increase the range and selectivity of new drugs, and there is a need for methods capable of…

Biomolecules · Quantitative Biology 2014-11-12 B. Amor , S. N. Yaliraki , R. Woscholski , M. Barahona

Protein representation and potential function are essential ingredients for studying proteins folding and protein prediction. We introduce a novel geometric representation of contact interactions using the edge simplices from alpha shape of…

Biological Physics · Physics 2007-05-23 Xiang Li , Changyu Hu , Jie Liang

The native three dimensional structure of a single protein is determined by the physico chemical nature of its constituent amino acids. The twenty different types of amino acids, depending on their physico chemical properties, can be…

Biomolecules · Quantitative Biology 2009-11-13 Md. Aftabuddin , S. Kundu

Hydrophobicity is thought to be one of the primary forces driving the folding of proteins. On average, hydrophobic residues occur preferentially in the core, whereas polar residues tends to occur at the surface of a folded protein. By…

Biomolecules · Quantitative Biology 2007-05-23 Susanne Moelbert , Eldon Emberly , Chao Tang

Allostery commonly refers to the mechanism that regulates protein activity through the binding of a molecule at a different, usually distal, site from the orthosteric site. The omnipresence of allosteric regulation in nature and its…

Biomolecules · Quantitative Biology 2022-07-18 Nan Wu , Sophia N. Yaliraki , Mauricio Barahona

A single protein molecule is regarded as a contact network of amino-acid residues. Some studies have indicated that this network is a small world network (SWN), while other results have implied that this is a fractal network (FN). However,…

Biological Physics · Physics 2009-11-13 Hidetoshi Morita , Mitsunori Takano

Function of proteins or a network of interacting proteins often involves communication between residues that are well separated in sequence. The classic example is the participation of distant residues in allosteric regulation.…

Biomolecules · Quantitative Biology 2007-05-23 Ruxandra I. Dima , D. Thirumalai

Allostery, the phenomenon by which the perturbation of a molecule at one site alters its behavior at a remote functional site, enables control over biomolecular function. Allosteric modulation is a promising avenue for drug discovery and is…

Biological Physics · Physics 2025-05-15 Maximilian Vossel , Bert L. de Groot , Aljaž Godec

Allostery is an intrinsic spatiotemporal property of all proteins, resulting from long range correlations in the order of several nanometers and time scales of nanoseconds. Information is carried asymmetrically from one part to another by…

Biomolecules · Quantitative Biology 2017-08-17 Aysima Hacisuleyman , Burak Erman

Models of protein energetics which neglect interactions between amino acids that are not adjacent in the native state, such as the Go model, encode or underlie many influential ideas on protein folding. Implicit in this simplification is a…

Biomolecules · Quantitative Biology 2009-10-08 Brian C. Gin , Juan P. Garrahan , Phillip L. Geissler

Proteins are an important class of biomolecules that serve as essential building blocks of the cells. Their three-dimensional structures are responsible for their functions. In this thesis we have investigated the protein structures using a…

Molecular Networks · Quantitative Biology 2007-11-19 Ganesh Bagler

E. Coli. dihydrofolate reductase (DHFR) undergoes conformational transitions between the closed (CS) and occluded (OS) states which, respectively, describe whether the active site is closed or occluded by the Met20 loop. A sequence-based…

Biomolecules · Quantitative Biology 2007-08-16 Jie Chen , Ruxandra I. Dima , D. Thirumalai

Allosteric proteins transmit a mechanical signal induced by binding a ligand. However, understanding the nature of the information transmitted and the architectures optimizing such transmission remains a challenge. Here we show using an…

Biological Physics · Physics 2018-08-01 Le Yan , Riccardo Ravasio , Carolina Brito , Matthieu Wyart