Mutational Tipping Points for Switching Protein Folds and Functions - Test2 - elhamkhani - TriplyDB

Mutational Tipping Points for Switching Protein Folds and Functions

Mutational Tipping Points for Switching Protein Folds and Functions

http://www.wikidata.org/entity/Q27677203

about

Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge Conservation of Protein Structure over Four Billion Years A comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometry Lessons from application of the UNRES force field to predictions of structures of CASP10 targets Computing the relative stabilities and the per-residue components in protein conformational changes.Virtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches.The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design The Role of Evolutionary Selection in the Dynamics of Protein Structure Evolution.A polymetamorphic protein.Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.Smooth functional transition along a mutational pathway with an abrupt protein fold switch.Biophysics of protein evolution and evolutionary protein biophysics Helical ambivalency induced by point mutations.Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.The albumin-binding domain as a scaffold for protein engineering.Implication of the cause of differences in 3D structures of proteins with high sequence identity based on analyses of amino acid sequences and 3D structures.Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases.Studying protein fold evolution with hybrids of differently folded homologs Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins Protein conformational switches: from nature to design.Comprehensive analysis of sequences of a protein switch.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Multisequence algorithm for coarse-grained biomolecular simulations: Exploring the sequence-structure relationship of proteins.Molecular dynamics simulations on the conformational transitions from the GA 98 (GA 88) to GB 98 (GB 88) proteins.Examination of the quality of various force fields and solvation models for the equilibrium simulations of GA88 and GB88.The energy landscape of a protein switch.Modeling Protein Folding Pathways GA/GB Fold switching may modulate fatty acid transfer from human serum albumin to bacteria

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Mutational Tipping Points for Switching Protein Folds and Functions

http://www.wikidata.org/entity/Q27677203

description

2012 nî lūn-bûn

@nan

2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի փետրվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

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name

Mutational Tipping Points for Switching Protein Folds and Functions

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Mutational Tipping Points for Switching Protein Folds and Functions

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Mutational Tipping Points for Switching Protein Folds and Functions

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type

label

Mutational Tipping Points for Switching Protein Folds and Functions

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Mutational Tipping Points for Switching Protein Folds and Functions

@en

Mutational Tipping Points for Switching Protein Folds and Functions

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Mutational Tipping Points for Switching Protein Folds and Functions

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Mutational Tipping Points for Switching Protein Folds and Functions

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Mutational Tipping Points for Switching Protein Folds and Functions

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J.STR.2011.11.018

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Mutational Tipping Points for Switching Protein Folds and Functions

@en

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Patrick A Alexander

http://www.w3.org/2001/XMLSchema#string

Philip N Bryan

http://www.w3.org/2001/XMLSchema#string

Yanan He

http://www.w3.org/2001/XMLSchema#string

Yihong Chen

http://www.w3.org/2001/XMLSchema#string

P2860

Consistent blind protein structure generation from NMR chemical shift data

The design and characterization of two proteins with 88% sequence identity but different structure and function

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition

Transitive homology-guided structural studies lead to discovery of Cro proteins with 40% sequence identity but different folds

Interconversion between two unrelated protein folds in the lymphotactin native state

A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G

NMR structures of two designed proteins with high sequence identity but different fold and function

A minimal sequence code for switching protein structure and function

Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG

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283-91

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scholarly article

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1083037

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10.1016/J.STR.2011.11.018

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2

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20

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221824218

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22325777

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protein folding

structural biology

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3278708

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