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Biological networks have evolved to be highly functional within uncertain environments while remaining extremely adaptable. One of the main contributors to the robustness and evolvability of biological networks is believed to be their…

Molecular Networks · Quantitative Biology 2008-02-14 Arend Hintze , Christoph Adami

Control of the living cell functions with remarkable reliability despite the stochastic nature of the underlying molecular networks -- a property presumably optimized by biological evolution. We here ask to what extent the property of a…

Molecular Networks · Quantitative Biology 2009-11-13 Stefan Braunewell , Stefan Bornholdt

Many aspects of the study of protein folding and dynamics have been affected by the recent advances in machine learning. Methods for the prediction of protein structures from their sequences are now heavily based on machine learning tools.…

Biological Physics · Physics 2019-11-25 Frank Noé , Gianni De Fabritiis , Cecilia Clementi

Geometric and structural constraints greatly restrict the selection of folds adapted by protein backbones, and yet, folded proteins show an astounding diversity in functionality. For structure to have any bearing on function, it is thus…

Biological Physics · Physics 2010-04-20 Brinda K. V. , Saraswathi Vishveshwara , Smitha Vishveshwara

Mechanically induced protein unfolding in the force-clamp apparatus is shown, in a coarse-grained model of ubiquitin, to have lognormal statistics above a treshold force and exponential below it. Correspondingly, the mean unfolding time is…

Biomolecules · Quantitative Biology 2007-05-23 Piotr Szymczak , Marek Cieplak

Theoretical studies of stretching proteins with slipknots reveal a surprising growth of their unfolding times when the stretching force crosses an intermediate threshold. This behavior arises as a consequence of the existence of alternative…

Biomolecules · Quantitative Biology 2010-01-05 Joanna I. Sułkowska , Piotr Sułkowski , José N. Onuchic

During their evolution, proteins explore sequence space via an interplay between random mutations and phenotypic selection. Here we build upon recent progress in reconstructing data-driven fitness landscapes for families of homologous…

Biomolecules · Quantitative Biology 2022-01-28 Matteo Bisardi , Juan Rodriguez-Rivas , Francesco Zamponi , Martin Weigt

In this work we propose a physical model of organismal evolution, where phenotype, organism life expectancy, is directly related to genotype i.e. the stability of its proteins which can be determined exactly in the model. Simulating the…

Populations and Evolution · Quantitative Biology 2007-05-23 Konstantin B. Zeldovich , Boris E. Shakhnovich , Eugene I. Shakhnovich

We provide evidence that the energy landscapes of folded proteins do not shift with temperature, but the onset of functional dynamics is associated with its effective sampling. The motion of the backbone is described by three distinct…

Soft Condensed Matter · Physics 2007-05-23 Canan Baysal , Ali Rana Atilgan

We suggest to simulate evolution of complex organisms constrained by the sole requirement of robustness in their expression patterns. This scenario is illustrated by evolving discrete logical networks with epigenetic properties. Evidence…

Statistical Mechanics · Physics 2007-05-23 Stefan Bornholdt , Kim Sneppen

The evolutionary trajectory of a protein through sequence space is constrained by function and three-dimensional (3D) structure. Residues in spatial proximity tend to co-evolve, yet attempts to invert the evolutionary record to identify…

Biomolecules · Quantitative Biology 2015-03-13 Debora S. Marks , Lucy J. Colwell , Robert Sheridan , Thomas A. Hopf , Andrea Pagnani , Riccardo Zecchina , Chris Sander

The structure and function of a protein are determined by its amino acid sequence. While random mutations change a protein's sequence, evolutionary forces shape its structural fold and biological activity. Studies have shown that neutral…

Biomolecules · Quantitative Biology 2024-11-15 Pranav Kantroo , Günter P. Wagner , Benjamin B. Machta

With the help of lattice Monte Carlo modelling of heteropolymers, we show that the necessary condition for a protein to fold on short call is to proceed through partially folded intermediates. These elementary structures are formed at an…

Condensed Matter · Physics 2007-05-23 R. A. Broglia , G. Tiana

A general theoretical framework is developed using free energy functional methods to understand the effects of heterogeneity in the folding of a well-designed protein. Native energetic heterogeneity arising from non-uniformity in native…

Disordered Systems and Neural Networks · Physics 2007-05-23 Steven S. Plotkin , Jose N. Onuchic

There are two contrasting explanations of sleep: as a proximate, essential physiological function or as an adaptive state of inactivity and these hypotheses remain widely debated. To investigate the adaptive significance of sleep, we…

Populations and Evolution · Quantitative Biology 2016-10-04 Jared M. Field , Michael B. Bonsall

The stability of a flexible fluid membrane containing a distribution of mobile, active proteins (e.g. proton pumps) is shown to depend on the structure and functional asymmetry of the proteins. A stable active membrane is in a…

Soft Condensed Matter · Physics 2009-10-31 Sriram Ramaswamy , John Toner , Jacques Prost

Robustness, the insensitivity of some of a biological system's functionalities to a set of distinct conditions, is intimately linked to fitness. Recent studies suggest that it may also play a vital role in enabling the evolution of species.…

Adaptation and Self-Organizing Systems · Physics 2011-12-15 James M Whitacre , Axel Bender

Proteins can sometimes be knotted, and for many reasons the study of knotted proteins is rapidly becoming very important. For example, it has been proposed that a knot increases the stability of a protein. Knots may also alter enzymatic…

Soft Condensed Matter · Physics 2009-07-02 Martin Lundgren , Antti J. Niemi

Gene expression and regulation rely on an apparently finely tuned set of reactions between some proteins and DNA. Such DNA-binding proteins have to find specific sequences on very long DNA molecules and they mostly do so in absence of any…

Biological Physics · Physics 2013-12-02 Maria Barbi , Fabien Paillusson

Expression level is known to be a strong determinant of a protein's rate of evolution. But the converse can also be true: evolutionary dynamics can affect expression levels of proteins. Having implications in both directions fosters the…

Populations and Evolution · Quantitative Biology 2021-06-09 Jacob Moran , Devon Finlay , Mikhail Tikhonov
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