Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.
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ARID1a-DNA interactions are required for promoter occupancy by SWI/SNFDevelopment of quantitative structure-binding affinity relationship models based on novel geometrical chemical descriptors of the protein-ligand interfaces.A conformational transition state accompanies tryptophan activation by B. stearothermophilus tryptophanyl-tRNA synthetase.HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method.
P2860
Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on September 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Evaluation of the relative sta ...... rotein Packing (SNAPP) method.
@en
Evaluation of the relative sta ...... od Analysis of Protein Packing
@nl
type
label
Evaluation of the relative sta ...... rotein Packing (SNAPP) method.
@en
Evaluation of the relative sta ...... od Analysis of Protein Packing
@nl
prefLabel
Evaluation of the relative sta ...... rotein Packing (SNAPP) method.
@en
Evaluation of the relative sta ...... od Analysis of Protein Packing
@nl
P2093
P2860
P356
P1433
P1476
Evaluation of the relative sta ...... rotein Packing (SNAPP) method.
@en
P2093
Douglas B Sherman
J Bruce Pitner
Shuxing Zhang
P2860
P304
P356
10.1002/PROT.20131
P407
P577
2004-09-01T00:00:00Z