Analysis of a data set of paired uncomplexed protein structures: New metrics for side-chain flexibility and model evaluation

Proteins: Structure, Function and Genetics

Volumn 43, Issue 3, 2001, Pages 271-279

  Zhao, Shanrong ^a   Goodsell, David S ^a   Olson, Arthur J ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Protein structure prediction; Side chain flexibility

Indexed keywords

ARGININE; GLUTAMINE; GLYCINE; LYSINE; METHIONINE; PROTEIN; SERINE;

ARTICLE; CRYSTAL STRUCTURE; DATA BASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

DATABASES, FACTUAL; MODELS, MOLECULAR; PROTEINS;

EID: 0035874146     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1038     Document Type: Article

References (11)

1. Dynamics of proteins: Elements and function
2. Comparison of conformational characteristics in structurally similar protein pairs
3. An analysis of conformational changes on protein-protein association: Implications for predictive docking
4. Side-chain flexibility in proteins upon ligand binding
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6. Comparison of two crystal structures of TGF-b2: The accuracy of refined protein structures
7. Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting
8. Reduced surface: An efficient way to compute molecular surfaces
9. Backbone-dependent rotomer library for proteins. Application to side-chain prediction
10. Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool
11. Improved modeling of side-chains in proteins with rotomer-based methods: A flexible rotomer model