NMR structures of two designed proteins with high sequence identity but different fold and function - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q27652181

about

A minimal sequence code for switching protein structure and function Metamorphic proteins mediate evolutionary transitions of structure Identification of Amino Acids that Account for Long-Range Interactions in Two Triosephosphate Isomerases from Pathogenic Trypanosomes Mutational Tipping Points for Switching Protein Folds and Functions Different contribution of conserved amino acids to the global properties of triosephosphate isomerases Constraint methods that accelerate free-energy simulations of biomolecules Artificial proteins as allosteric modulators of PDZ3 and SH3 in two-domain constructs: A computational characterization of novel chimeric proteins.Computing the relative stabilities and the per-residue components in protein conformational changes.ChSeq: A database of chameleon sequences.Discrete-continuous duality of protein structure space.I-TASSER: fully automated protein structure prediction in CASP8 De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds Diversity of protein structures and difficulties in fold recognition: the curious case of protein G.Re-engineering a beta-lactamase using prototype peptides from a library of local structural motifs.A nuclear magnetic resonance based approach to accurate functional annotation of putative enzymes in the methanogen Methanosarcina acetivorans.Networking the nucleus.Proteins that switch folds Sequence and structure continuity of evolutionary importance improves protein functional site discovery and annotation.Take home lessons from studies of related proteins The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function.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.Studying protein fold evolution with hybrids of differently folded homologs Folding pathways of proteins with increasing degree of sequence identities but different structure and function.HASH: a program to accurately predict protein Hα shifts from neighboring backbone shifts How does a simplified-sequence protein fold?Is protein classification necessary? Toward alternative approaches to function annotation.Homology modelling and spectroscopy, a never-ending love story.Protein conformational switches: from nature to design.Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.The spectrum of biomolecular states and motions.Better theoretical models and protein design experiments can help to understand protein folding.Ab initio folding of extended α-helix: a theoretical study about the role of electrostatic polarization in the folding of helical structures.Search for identical octapeptides in unrelated proteins: Structural plasticity revisited.Replica exchange molecular dynamics simulation of structure variation from α/4β-fold to 3α-fold protein.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.Insenstivity to Close Contacts and Inability to Predict Protein Foldability Modeling Protein Folding Pathways

P2860

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P2860

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

http://www.wikidata.org/entity/Q27652181

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

NMR structures of two designed ...... ut different fold and function

@ast

NMR structures of two designed ...... ut different fold and function

@en

NMR structures of two designed ...... ut different fold and function

@nl

type

label

NMR structures of two designed ...... ut different fold and function

@ast

NMR structures of two designed ...... ut different fold and function

@en

NMR structures of two designed ...... ut different fold and function

@nl

prefLabel

NMR structures of two designed ...... ut different fold and function

@ast

NMR structures of two designed ...... ut different fold and function

@en

NMR structures of two designed ...... ut different fold and function

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

NMR structures of two designed ...... ut different fold and function

@en

P2093

Patrick 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

Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions

Convergent evolution among immunoglobulin G-binding bacterial proteins

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

Evolution of a protein fold in vitro

Core mutations switch monomeric protein GB1 into an intertwined tetramer

Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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14412-7

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scholarly article

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10.1073/PNAS.0805857105

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38

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105

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23262428

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18796611

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P921

protein folding

P932

2567172

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