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Although several synonymous codons can encode the same aminoacid, this symmetry is generally broken in natural genetic systems. In this article, we show that the symmetry breaking can result from selective pressures due to the violation of…

adap-org · Physics 2008-02-03 S. Vera , H. Waelbroeck

Proteins are composed of chains of amino acids that fold into complex three-dimensional structures. Several key features, such as the radius of gyration, fraction of core amino acids $f_{\rm core}$, packing fraction $\langle \phi\rangle$ of…

Soft Condensed Matter · Physics 2025-11-07 Jack A. Logan , Jacob Sumner , Alex T. Grigas , Mark D. Shattuck , Corey S. OHern

Protein structure tokenization converts 3D structures into discrete or vectorized representations, enabling the integration of structural and sequence data. Despite many recent works on structure tokenization, the properties of the…

Machine Learning · Computer Science 2025-11-14 Zijing Liu , Bin Feng , He Cao , Yu Li

Given the amino acid sequence of a protein, researchers often infer its structure and function by finding homologous, or evolutionarily-related, proteins of known structure and function. Since structure is typically more conserved than…

Computational Engineering, Finance, and Science · Computer Science 2015-03-23 Noah M. Daniels

Proteins have regular tertiary structures but irregular amino acid sequences. This made it very difficult to decode the structural information in the protein sequences. Here we demonstrate that many small alpha protein domains have hidden…

Biomolecules · Quantitative Biology 2007-05-23 Ruizhen Xu , Yanzhao Huang , Mingfen Li , Hanlin Chen , Yi Xiao

Evolution in its course found a variety of solutions to the same optimisation problem. The advent of high-throughput genomic sequencing has made available extensive data from which, in principle, one can infer the underlying structure on…

Quantitative Methods · Quantitative Biology 2016-04-12 Silvia Grigolon , Silvio Franz , Matteo Marsili

Proteins must bind to specific other proteins in vivo in order to function. The proteins must bind only to one or a few other proteins of the of order a thousand proteins typically present in vivo. Using a simple model of a protein,…

Biomolecules · Quantitative Biology 2007-05-23 Richard P. Sear

We present a geometrical analysis of the protrusion statistics of side chains in more than 4,000 high-resolution protein structures. We employ a coarse-grained representation of the protein backbone viewed as a linear chain of C{\alpha}…

Soft Condensed Matter · Physics 2024-01-29 Tatjana Škrbić , Achille Giacometti , Trinh X. Hoang , Amos Maritan , Jayanth R. Banavar

Proteins are essential for life, and their structure determines their function. The protein secondary structure is formed by the folding of the protein primary structure, and the protein tertiary structure is formed by the bending and…

Biomolecules · Quantitative Biology 2024-03-11 Yanlin Zhou , Kai Tan , Xinyu Shen , Zheng He , Haotian Zheng

Protein-protein interactions (protein functionalities) are mediated by water, which compacts individual proteins and promotes close and temporarily stable large-area protein-protein interfaces. Proteins are peptide chains decorated by amino…

Soft Condensed Matter · Physics 2008-02-26 J. C. Phillips

The computational prediction of a protein structure from its sequence generally relies on a method to assess the quality of protein models. Most assessment methods rank candidate models using heavily engineered structural features, defined…

Biomolecules · Quantitative Biology 2018-11-26 Georgy Derevyanko , Sergei Grudinin , Yoshua Bengio , Guillaume Lamoureux

Inverse protein folding is challenging due to its inherent one-to-many mapping characteristic, where numerous possible amino acid sequences can fold into a single, identical protein backbone. This task involves not only identifying viable…

Quantitative Methods · Quantitative Biology 2023-11-08 Kai Yi , Bingxin Zhou , Yiqing Shen , Pietro Liò , Yu Guang Wang

Specific protein-protein interactions are crucial in the cell, both to ensure the formation and stability of multi-protein complexes, and to enable signal transduction in various pathways. Functional interactions between proteins result in…

Biological Physics · Physics 2016-11-21 Anne-Florence Bitbol , Robert S. Dwyer , Lucy J. Colwell , Ned S. Wingreen

The design of novel proteins has many applications but remains an attritional process with success in isolated cases. Meanwhile, deep learning technologies have exploded in popularity in recent years and are increasingly applicable to…

Biomolecules · Quantitative Biology 2018-11-07 Joe G Greener , Lewis Moffat , David T Jones

In this work it is shown that 20 canonical amino acids (AAs) within genetic code appear to be a whole system with strict AAs positions; more exactly, with AAs ordinal number in three variants; first variant 00-19, second 00-21 and third…

Other Quantitative Biology · Quantitative Biology 2015-06-26 Zvonimir M. Damjanovic , Miloje M. Rakocevic

The idea that structural disorder might be a novel mechanism of protein interaction is widespread in the Literature, although the number of statistically significant structural studies supporting this is surprisingly low. At variance with…

Disordered Systems and Neural Networks · Physics 2021-03-01 Beatriz Seoane , Alessandra Carbone

A method based on mapping a symbolic sequence into a set of patterns (strings resulting from the sequence parsing) is proposed as a tool for the reconstruction of ancestral sequences. The set union of patterns comprises all the patterns…

Genomics · Quantitative Biology 2015-04-16 Bohdan Kozarzewski

The protein folding problem must ultimately be solved on all length scales from the atomic up through a hierarchy of complicated structures. By analyzing the stability of the folding process using physics and mathematics, this paper shows…

Biological Physics · Physics 2015-05-28 Walter Simmons , Joel L. Weiner

The network paradigm is increasingly used to describe the topology and dynamics of complex systems. Here we review the results of the topological analysis of protein structures as molecular networks describing their small-world character,…

Biomolecules · Quantitative Biology 2007-06-10 Csaba Bode , Istvan A. Kovacs , Mate S. Szalay , Robin Palotai , Tamas Korcsmaros , Peter Csermely

We study the impact of mutations (changes in amino acid sequence) on the thermodynamics of simple protein-like heteropolymers consisting of N monomers, representing the amino acid sequence. The sequence is designed to fold into its native…

Condensed Matter · Physics 2009-10-30 G. Tiana , R. A. Broglia , H. E. Roman , E. Vigezzi , E. Shakhnovich