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Related papers: Elements of Coevolution in Biological Sequences

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Numerous experiments demonstrate a high level of promiscuity and structural disorder in organismal proteomes. Here we ask the question what makes a protein promiscuous, i.e., prone to non-specific interactions, and structurally disordered.…

Biomolecules · Quantitative Biology 2011-05-10 Ariel Afek , Eugene I. Shakhnovich , David B. Lukatsky

The analysis of the three-dimensional structure of proteins is an important topic in molecular biochemistry. Structure plays a critical role in defining the function of proteins and is more strongly conserved than amino acid sequence over…

Applications · Statistics 2015-01-19 Abel Rodriguez , Scott C. Schmidler

In the protein sequence space, natural proteins form clusters of families which are characterized by their unique native folds whereas the great majority of random polypeptides are neither clustered nor foldable to unique structures. Since…

Biomolecules · Quantitative Biology 2018-02-06 Akira R. Kinjo

Composed of amino acid chains that influence how they fold and thus dictating their function and features, proteins are a class of macromolecules that play a central role in major biological processes and are required for the structure,…

Quantitative Methods · Quantitative Biology 2022-07-15 Aaron Wang

Proteins are a matter of dual nature. As a physical object, a protein molecule is a folded chain of amino acids with multifarious biochemistry. But it is also an instantiation along an evolutionary trajectory determined by the function…

Biomolecules · Quantitative Biology 2019-09-04 Jean-Pierre Eckmann , Jacques Rougemont , Tsvi Tlusty

Biological diversity has evolved despite the essentially infinite complexity of protein sequence space. We present a hierarchical approach to the efficient searching of this space and quantify the evolutionary potential of our approach with…

Statistical Mechanics · Physics 2009-10-31 Leonard D. Bogarad , Michael W. Deem

Statistical coupling analysis (SCA) is a method for analyzing multiple sequence alignments that was used to identify groups of coevolving residues termed "sectors". The method applies spectral analysis to a matrix obtained by combining…

Biomolecules · Quantitative Biology 2015-06-19 Tiberiu Tesileanu , Lucy J. Colwell , Stanislas Leibler

We study two mechanisms for the formation of protein patterns near membranes of living cells by mathematical modelling. Self-assembly of protein domains by electrostatic lipid-protein interactions is contrasted with self-organization due to…

Cell Behavior · Quantitative Biology 2007-05-23 Karin John , Markus Baer

Measuring gene expression simultaneously in both hosts and symbionts offers a powerful approach to explore the biology underlying species interactions. Such dual or simultaneous RNAseq approaches have primarily been used to gain insight…

Populations and Evolution · Quantitative Biology 2022-06-28 Amanda K Hund , Peter Tiffin , Jean-Gabriel Young , Daniel I Bolnick

Non-coding RNAs are ubiquitous, but the discovery of new RNA gene sequences far outpaces research on their structure and functional interactions. We mine the evolutionary sequence record to derive precise information about function and…

Biomolecules · Quantitative Biology 2016-04-22 Caleb Weinreb , Adam J. Riesselman , John B. Ingraham , Torsten Gross , Chris Sander , Debora S. Marks

Complex interactions between genes or proteins contribute a substantial part to phenotypic evolution. Here we develop an evolutionarily grounded method for the cross-species analysis of interaction networks by {\em alignment}, which maps…

Molecular Networks · Quantitative Biology 2009-11-13 Johannes Berg , Michael Lässig

The primary structure of proteins, that is their sequence, represents one of the most abundant set of experimental data concerning biomolecules. The study of correlations in families of co--evolving proteins by means of an inverse…

Biomolecules · Quantitative Biology 2015-06-16 Sara Lui , Guido Tiana

The correlations of primary and secondary structures were analyzed using proteins with known structure from Protein Data Bank. The correlation values of amino acid type and the eight secondary structure types at distant position were…

Biomolecules · Quantitative Biology 2007-05-23 Sasa Malkov , Miodrag V. Zivkovic , Milos V. Beljanski , Snezana D. Zaric

Evolution of genetic code is studied as the change in the choice of enzymes that are used to synthesize amino acids from the genetic information of nucleic acids. We propose the following theory: the differentiation of physiological states…

Adaptation and Self-Organizing Systems · Physics 2007-05-23 H. Takagi , K. Kaneko , T. Yomo

Since protein mutations are the main driving force of evolution at the molecular level, a proper analysis of them (and the factors controlling them) will enable us to find a response to several crucial queries in evolutionary biology. Among…

Populations and Evolution · Quantitative Biology 2024-12-24 J. A. Vila

We propose a model that explains the hierarchical organization of proteins in fold families. The model, which is based on the evolutionary selection of proteins by their native state stability, reproduces patterns of amino acids conserved…

Statistical Mechanics · Physics 2007-05-23 Nikolay V. Dokholyan , Eugene I. Shakhnovich

The correlations between the sequence of monomers in a polymer and its three-dimensional structure is a grand challenge in polymer science and biology. The properties and functions of macromolecules depend on their 3D shape that has…

Materials Science · Physics 2021-07-15 Ashwin A Bale , Tarak K Patra

How proteins fold remains a central unsolved problem in biology. While the idea of a folding code embedded in the amino acid sequence was introduced more than 6 decades ago, this code remains undefined. While we now have powerful predictive…

Biomolecules · Quantitative Biology 2025-11-04 Carlos Bustamante , Christian Kaiser , Erik Lindahl , Robert Sosa , Giovanni Volpe

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

Upon the covalent-bonding hybrid of the nitrogen atoms taken as a measure for the structural regularity in nucleobases, it can be identified that the internal relation within the 20 amino acids follows a cooperative vector-in-space addition…

Biomolecules · Quantitative Biology 2007-05-23 Chi Ming Yang
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