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Related papers: Protein Adaptive Plasticity and Night Vision

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Self-organized criticality (SOC) is a popular concept that has been the subject of more than 3000 articles in the last 25 years. Here we show that SOC may enable theory to connect standard Web-based (BLAST) short-range amino acid (aa)…

Soft Condensed Matter · Physics 2011-02-14 J. C. Phillips

Proteins appear to be the most dramatic natural example of self-organized criticality (SOC), a concept that explains many otherwise apparently unlikely phenomena. Protein conformational functionality is often dominated by long-range…

Soft Condensed Matter · Physics 2010-11-19 J. C. Phillips

Proteins appear to be the most dramatic natural example of self-organized criticality (SOC), a concept that explains many otherwise apparently unlikely phenomena. Protein functionality is dominated by long range hydro(phobic/philic)…

Soft Condensed Matter · Physics 2008-08-19 J. C. Phillips

The behavior of disease-linked mutations of membrane proteins is especially simple in rhodopsin, where they are well-studied, as they are responsible for retinitis pigmentosa, RP (retinal degeneration). Here we show that the frequency of…

Soft Condensed Matter · Physics 2015-06-03 J. C. Phillips

We focus here on the scaling properties of small interspecies differences between red cone opsin transmembrane proteins, using a hydropathic elastic roughening tool previously applied to the rhodopsin rod transmembrane proteins. This tool…

Soft Condensed Matter · Physics 2012-02-24 J. C. Phillips

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

The ability of a protein to recognise multiple independent target conformations was demonstrated in [1]. Here we consider the recognition of correlated configurations, which we apply to funnel design for a single conformation. The maximum…

Soft Condensed Matter · Physics 2007-05-23 Robin C Ball , Thomas M A Fink

When an object moves smoothly across a field of view, the identify of the object is unchanged, but the activation pattern of the photoreceptors on the retina changes drastically. One of the major computational roles of our visual system is…

Neurons and Cognition · Quantitative Biology 2014-04-23 Minjoon Kouh

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

One of the main trend in to date research and development is the miniaturization of electronic devices. In this perspective, integrated nanodevices based on proteins or biomolecules are attracting a major interest. In fact, it has been…

Quantitative Methods · Quantitative Biology 2015-06-26 E. Alfinito , C. Pennetta , L. Reggiani

Improving the ability to predict protein function can potentially facilitate research in the fields of drug discovery and precision medicine. Technically, the properties of proteins are directly or indirectly reflected in their sequence and…

Biomolecules · Quantitative Biology 2024-11-19 Runze Ma , Chengxin He , Huiru Zheng , Xinye Wang , Haiying Wang , Yidan Zhang , Lei Duan

In protein folding the term plasticity refers to the number of alternative folding pathways encountered in response to free energy perturbations such as those induced by mutation. Here we explore the relation between folding plasticity and…

Biomolecules · Quantitative Biology 2008-09-09 P. F. N. Faisca , C. M. Gomes

Rhodopsin is a G-protein coupled receptor found in retinal rod cells, where it mediates monocrhromatic vision in dim light. It is one of the most studied proteins with thousands of reviewed entries in Uniprot. It has seven transmembrane…

Other Quantitative Biology · Quantitative Biology 2023-06-01 J. C. Phillips

Novel numerical techniques, validated by an analysis of barnase and chymotrypsin inhibitor, are used to elucidate the paramount role played by the geometry of the protein backbone in steering the folding to the correct native state. It is…

Statistical Mechanics · Physics 2009-10-31 Cristian Micheletti , Jayanth R. Banavar , Amos Maritan , Flavio Seno

The increasing interest in photoactivated proteins as natural replacement of standard inorganic materials in photocells drives to the compared analysis of bacteriorhodopsin and proteorhodopsin, two widely diffused proteins belonging to the…

Biological Physics · Physics 2015-06-16 E Alfinito , J Pousset , L Reggiani , K Lee

Native protein folds often have a high degree of symmetry. We study the relationship between the symmetries of native proteins, and their designabilities -- how many different sequences encode a given native structure. Using a…

Statistical Mechanics · Physics 2009-10-31 Tairan Wang , Jonathan Miller , Ned S. Wingreen , Chao Tang , Ken A. Dill

Protein sequence design must balance designability, defined as the ability to recover a target backbone, with multiple, often competing, developability properties such as solubility, thermostability, and expression. Existing approaches…

Machine Learning · Computer Science 2026-03-11 Xiaoyang Hou , Junqi Liu , Chence Shi , Xin Liu , Zhi Yang , Jian Tang

Protein structures can be studied as complex networks of interacting amino acids. We study proteins of different structural classes from the network perspective. Our results indicate that proteins, regardless of their structural class, show…

Molecular Networks · Quantitative Biology 2007-11-19 Ganesh Bagler , Somdatta Sinha

Proteins play a central role in biology from immune recognition to brain activity. While major advances in machine learning have improved our ability to predict protein structure from sequence, determining protein function from structure…

Protein-protein interactions (protein functionalities) are mediated by water, which compacts individual proteins and promotes close and temporarily stable large-area protein-protein interfaces. In their classic paper Kyte and Doolittle (KD)…

Soft Condensed Matter · Physics 2009-11-13 Alexander E. Kister , James C. Phillips
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