Comparison of X-ray and NMR structures: Is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?

Proteins: Structure, Function and Genetics

Volumn 60, Issue 1, 2005, Pages 139-147

  Garbuzynskiy, Sergiy O ^a   Melnik, Bogdan S ^a   Lobanov, Michail Yu ^a   Finkelstein, Alexei V ^a   Galzitskaya, Oxana V ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

Accessible surface area; Hydrogen bonds; Interresidue contacts; Structural alignment; X ray and NMR protein structures

Indexed keywords

PROTEIN;

ARTICLE; DATA BASE; HYDROGEN BOND; INTERMETHOD COMPARISON; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; SURFACE PROPERTY; X RAY ANALYSIS;

ANIMALS; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; DATABASES, PROTEIN; HUMANS; HYDROGEN BONDING; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEINS;

EID: 19544370004     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20491     Document Type: Article

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