Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values. - Wikidata - wikimedia - TriplyDB

Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.

Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.

http://www.wikidata.org/entity/Q38632179

about

Atomic-level characterization of the structural dynamics of proteins Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins.Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein Constrained proper sampling of conformations of transition state ensemble of protein folding.Folding pathways of proteins with increasing degree of sequence identities but different structure and function.How quickly can a β-hairpin fold from its transition state?The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis.pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Ratcheted molecular-dynamics simulations identify efficiently the transition state of protein folding.

P2860

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P2860

Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.

http://www.wikidata.org/entity/Q38632179

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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name

Characterisation of transition ...... edium' and 'low' {Phi}-values.

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type

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Characterisation of transition ...... edium' and 'low' {Phi}-values.

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Characterisation of transition ...... edium' and 'low' {Phi}-values.

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Protein Engineering Design and Selection

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Characterisation of transition ...... edium' and 'low' {Phi}-values.

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Christian D Geierhaas

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Jane Clarke

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P2860

The Protein Data Bank

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

Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein

Structure in solution of the major cold-shock protein from Bacillus subtilis

Effective energy function for proteins in solution

Self-consistent determination of the transition state for protein folding: application to a fibronectin type III domain.

Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

The folding transition state of the cold shock protein is strongly polarized.

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215-222

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scholarly article

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10.1093/PROTEIN/GZM092

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3

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21

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Michele Vendruscolo

Xavier Salvatella

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2008-03-01T00:00:00Z

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5553595

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18299294

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protein folding

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2397543

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