The relationship between relative solvent accessibility and evolutionary rate in protein evolution. - Test2 - elhamkhani - TriplyDB

The relationship between relative solvent accessibility and evolutionary rate in protein evolution.

The relationship between relative solvent accessibility and evolutionary rate in protein evolution.

http://www.wikidata.org/entity/Q35065511

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Causes of evolutionary rate variation among protein sites Functional Sites Induce Long-Range Evolutionary Constraints in Enzymes Diversification and coevolution of the ghrelin/growth hormone secretagogue receptor system in vertebrates Amino-acid site variability among natural and designed proteins Site-specific structural constraints on protein sequence evolutionary divergence: local packing density versus solvent exposure.Parallel dynamics and evolution: Protein conformational fluctuations and assembly reflect evolutionary changes in sequence and structure.The evolution of protein structures and structural ensembles under functional constraint.Predicting evolutionary site variability from structure in viral proteins: buriedness, packing, flexibility, and design.Roles of solvent accessibility and gene expression in modeling protein sequence evolution The utility of protein structure as a predictor of site-wise dN/dS varies widely among HIV-1 proteins.Maintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million Years Dissecting the roles of local packing density and longer-range effects in protein sequence evolution Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.The Impact of Native State Switching on Protein Sequence Evolution.Computational prediction of the tolerance to amino-acid deletion in green-fluorescent protein.On the Relationship between Residue Structural Environment and Sequence Conservation in Proteins.Modeling coding-sequence evolution within the context of residue solvent accessibility.Integrating sequence variation and protein structure to identify sites under selection Independent effects of protein core size and expression on residue-level structure-evolution relationships.A mechanistic stress model of protein evolution accounts for site-specific evolutionary rates and their relationship with packing density and flexibility.The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin.Local packing density is the main structural determinant of the rate of protein sequence evolution at site level.Biophysical and structural considerations for protein sequence evolution Too packed to change: side-chain packing and site-specific substitution rates in protein evolution Semirational Directed Evolution of Loop Regions in Aspergillus japonicus β-Fructofuranosidase for Improved Fructooligosaccharide Production Structure and age jointly influence rates of protein evolution.Determinants of exon-level evolutionary rates in Arabidopsis species.Long-Range Epistasis Mediated by Structural Change in a Model of Ligand Binding Proteins Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV's Envelope Protein on Viral Replication in Cell Culture Quantitative residue-level structure-evolution relationships in the yeast membrane proteome Capturing the mutational landscape of the beta-lactamase TEM-1.Three independent determinants of protein evolutionary rate.Calculating site-specific evolutionary rates at the amino-acid or codon level yields similar rate estimates.Extensively Parameterized Mutation-Selection Models Reliably Capture Site-Specific Selective Constraint.Relationship between protein thermodynamic constraints and variation of evolutionary rates among sites.A Comparison of One-Rate and Two-Rate Inference Frameworks for Site-Specific dN/dS Estimation.Intermediate divergence levels maximize the strength of structure-sequence correlations in enzymes and viral proteins.Structural evolution of proteinlike heteropolymers.Membrane environment imposes unique selection pressures on transmembrane domains of G protein-coupled receptors A sparse autoencoder-based deep neural network for protein solvent accessibility and contact number prediction.

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P2860

The relationship between relative solvent accessibility and evolutionary rate in protein evolution.

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2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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The relationship between relat ...... ary rate in protein evolution.

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The relationship between relat ...... ary rate in protein evolution.

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P2860

The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system

The relation between the divergence of sequence and structure in proteins

On the probability of fixation of mutant genes in a population

Thermodynamic prediction of protein neutrality

MUSCLE: multiple sequence alignment with high accuracy and high throughput

A database of protein structure families with common folding motifs

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach

PAML 4: phylogenetic analysis by maximum likelihood

Protein tolerance to random amino acid change

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Duncan C Ramsey

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protein evolution

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