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A minimal sequence code for switching protein structure and function

A minimal sequence code for switching protein structure and function

http://www.wikidata.org/entity/Q27658235

about

Comparative analysis of the quality of a global algorithm and a local algorithm for alignment of two sequences Metamorphic proteins mediate evolutionary transitions of structure An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor Mutational Tipping Points for Switching Protein Folds and Functions Divergent evolution of protein conformational dynamics in dihydrofolate reductase.Constraint methods that accelerate free-energy simulations of biomolecules Interdomain contacts control folding of transcription factor RfaH.Computing the relative stabilities and the per-residue components in protein conformational changes.Quantitative theory of hydrophobic effect as a driving force of protein structure Virtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.CSI 2.0: a significantly improved version of the Chemical Shift Index.The virtue of innovation: innovation through the lenses of biological evolution Evolution, energy landscapes and the paradoxes of protein folding.ChSeq: A database of chameleon sequences.De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds 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.Protein secondary structure prediction using a small training set (compact model) combined with a Complex-valued neural network approach.Predicting disease-associated substitution of a single amino acid by analyzing residue interactions.The Role of Evolutionary Selection in the Dynamics of Protein Structure Evolution.Structural gymnastics of multifunctional metamorphic proteins.Evolutionary bridges to new protein folds: design of C-terminal Cro protein chameleon sequences.Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.Biophysical mechanisms for large-effect mutations in the evolution of steroid hormone receptors.Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustness Investigating homology between proteins using energetic profiles Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.Evolution: a guide to perturb protein function and networks Proteins that switch folds Bootstrapping new protein folds Smooth functional transition along a mutational pathway with an abrupt protein fold switch.Biophysics of protein evolution and evolutionary protein biophysics Evolutionary biochemistry: revealing the historical and physical causes of protein properties.The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function.Single nucleotide variations: biological impact and theoretical interpretation.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.Search and analysis of identical reverse octapeptides in unrelated proteins.

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P2860

A minimal sequence code for switching protein structure and function

http://www.wikidata.org/entity/Q27658235

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

A minimal sequence code for switching protein structure and function

@ast

A minimal sequence code for switching protein structure and function

@en

A minimal sequence code for switching protein structure and function

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type

label

A minimal sequence code for switching protein structure and function

@ast

A minimal sequence code for switching protein structure and function

@en

A minimal sequence code for switching protein structure and function

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prefLabel

A minimal sequence code for switching protein structure and function

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A minimal sequence code for switching protein structure and function

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A minimal sequence code for switching protein structure and function

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A minimal sequence code for switching protein structure and function

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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

Convergent evolution among immunoglobulin G-binding bacterial proteins

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

Core mutations switch monomeric protein GB1 into an intertwined tetramer

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

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

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

Sequence determinants of a conformational switch in a protein structure.

The network of sequence flow between protein structures.

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