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Volumn 23, Issue 2, 2002, Pages 139-150
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Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR
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Author keywords
Aggregation; Anisotropy; Exchange; Hydrodynamic calculations; Protein NMR; Relaxation; Rotational diffusion
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Indexed keywords
GLOBULAR PROTEIN;
NITROGEN;
PROTEIN;
ANISOTROPY;
ARTICLE;
ATOM;
CALCULATION;
COMPUTER PROGRAM;
CONTROLLED STUDY;
DATA ANALYSIS;
HYDRODYNAMICS;
MOLECULAR MODEL;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PREDICTION;
PRIORITY JOURNAL;
PROTEIN STRUCTURE;
RADIUS;
ALGORITHM;
CHEMICAL STRUCTURE;
CHEMISTRY;
COMPARATIVE STUDY;
METHODOLOGY;
NUCLEAR MAGNETIC RESONANCE;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
STRUCTURE ACTIVITY RELATION;
ALGORITHMS;
ANISOTROPY;
MODELS, MOLECULAR;
NITROGEN ISOTOPES;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEINS;
SOFTWARE;
STRUCTURE-ACTIVITY RELATIONSHIP;
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EID: 0035996729
PISSN: 09252738
EISSN: None
Source Type: Journal
DOI: 10.1023/A:1016359412284 Document Type: Article |
Times cited : (79)
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References (52)
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