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Related papers: A modular Fibonacci sequence in proteins

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All known terrestrial proteins are coded as continuous strings of ~20 amino acids. The patterns formed by the repetitions of elements in groups of finite sequences describes the natural architectures of protein families. We present a method…

Biomolecules · Quantitative Biology 2018-07-30 Pablo Turjanski , Diego U. Ferreiro

Some natural proteins display recurrent structural patterns. Despite being highly similar at the tertiary structure level, repetitions within a single repeat protein can be extremely variable at the sequence level. We propose a mathematical…

Biomolecules · Quantitative Biology 2015-10-12 Pablo Turjanski , R. Gonzalo Parra , Rocío Espada , Verónica Becher , Diego U. Ferreiro

The coding space of protein sequences is shaped by evolutionary constraints set by requirements of function and stability. We show that the coding space of a given protein family--the total number of sequences in that family--can be…

Biomolecules · Quantitative Biology 2020-11-20 Jacopo Marchi , Ezequiel A. Galpern , Rocio Espada , Diego U. Ferreiro , Aleksandra M. Walczak , Thierry Mora

This work aims at showing the relevance and the applications possibilities of the Fibonacci sequence, and also its q-deformed or quantum extension, in the study of the genetic code(s). First, after the presentation of a new formula, an…

Other Quantitative Biology · Quantitative Biology 2015-10-06 Tidjani Negadi

The stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into 5the ``native'' conformation. By a complete enumeration of the…

Soft Condensed Matter · Physics 2009-10-31 R. A Broglia , G. Tiana , H. E. Roman , E. Vigezzi , E. I. Shakhnovich

In the course of evolution, proteins undergo important changes in their amino acid sequences, while their three-dimensional folded structure and their biological function remain remarkably conserved. Thanks to modern sequencing techniques,…

Biomolecules · Quantitative Biology 2019-10-07 Simona Cocco , Christoph Feinauer , Matteo Figliuzzi , Remi Monasson , Martin Weigt

We seek to understand the interplay between amino acid sequence and local structure in proteins. Are some amino acids unique in their ability to fit harmoniously into certain local structures? What is the role of sequence in sculpting the…

Biomolecules · Quantitative Biology 2021-01-29 Tatjana Škrbić , Amos Maritan , Achille Giacometti , Jayanth R. Banavar

Background:Prediction of protein three-dimensional structures from amino acid sequences is a long-standing goal in computational/molecular biology. The successful discrimination of protein folds would help to improve the accuracy of protein…

Biomolecules · Quantitative Biology 2007-05-23 Y-h. Taguchi , M. Michael Gromiha

The observed correlations between pairs of homologous protein sequences are typically explained in terms of a Markovian dynamic of amino acid substitution. This model assumes that every location on the protein sequence has the same…

Biomolecules · Quantitative Biology 2007-05-23 Gavin E. Crooks , Steven E. Brenner

Mapping between sequence and structure is currently an open problem in structural biology. Despite many experimental and computational efforts it is not clear yet how the structure is encoded in the sequence. Answering this question may…

Biomolecules · Quantitative Biology 2013-10-08 Iddo Friedberg

The folding characteristics of sequences reduced with a possibly simplified representation of five types of residues are shown to be similar to their original ones with the natural set of residues (20 types or 20 letters). The reduced…

Biological Physics · Physics 2009-11-06 Jun Wang , Wei Wang

In this Communication we present statistical analysis of conservation profiles in families of homologous sequences for nine proteins whose folding nucleus was determined by protein engineering methods. We show that in all but one protein…

Biological Physics · Physics 2007-05-23 Leonid Mirny , Eugene Shakhnovich

Proteins are large biomolecules that regulate all living organisms and consist of one or several chains. The primary structure of a protein chain is a sequence of amino acid residues whose three main atoms (alpha-carbon, nitrogen, and…

Computational Geometry · Computer Science 2025-12-30 Olga Anosova , Alexey Gorelov , William Jeffcott , Ziqiu Jiang , Vitaliy Kurlin

It has been conjectured that evolution exerted pressure to preserve amino acids bearing thermodynamic, kinetic, and functional roles. In this letter we show that the physical requirement to maintain protein stability gives rise to a…

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

A novel scheme is introduced to capture the spatial correlations of consecutive amino acids in naturally occurring proteins. This knowledge-based strategy is able to carry out optimally automated subdivisions of protein fragments into…

Soft Condensed Matter · Physics 2007-05-23 Cristian Micheletti , Flavio Seno , Amos Maritan

The number of atoms in the four ribonucleotides uridine monophosphate, cytidine monophosphate, adenine monophosphate and guanine monophosphate is taken as a key parameter. A mathematical relation describing the condensation of the three…

Other Quantitative Biology · Quantitative Biology 2014-06-25 Tidjani Negadi

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

A representation of the genetic code as a six-dimensional Boolean hypercube is proposed. It is assumed here that this structure is the result of the hierarchical order of the interaction energies of the bases in codon-anticodon recognition.…

Soft Condensed Matter · Physics 2007-05-23 Miguel A. Jimenez-Montano , Carlos R. de la Mora-Basanez , Thorsten Poeschel

Protein sequences serve as a natural record of the evolutionary constraints that shape their functional structures. We show that it is possible to use only sequence information to go beyond predicting native structures and global stability…

Biomolecules · Quantitative Biology 2025-07-02 Ezequiel A. Galpern , Ernesto A. Roman , Diego U. Ferreiro

The spectrum and scale of fluctuations in protein structures affect the range of cell phenomena, including stability of protein structures or their fragments, allosteric transitions and energy transfer. The study presents a…

Biomolecules · Quantitative Biology 2015-05-13 Anatoly M. Ruvinsky , Ilya A. Vakser
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