Variation of Molecular Alignment as a Means of Resolving Orientational Ambiguities in Protein Structures from Dipolar Couplings

Journal of Magnetic Resonance

Volumn 143, Issue 2, 2000, Pages 402-406

  Al Hashimi, H M ^a,b   Valafar, H ^a   Terrell, M ^a   Zartler, E R ^a   Eidsness, M K ^a   Prestegard, J H ^a  

^a UNIVERSITY OF GEORGIA   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

Bicelle; NMR; Order matrix; Protein fold; Rubredoxin

Indexed keywords

BACTERIAL PROTEIN; HYDROGEN; NITROGEN; PROTEIN; RUBREDOXIN; RUBREDOXIN PROTEIN, CLOSTRIDIUM PASTEURIANUM;

ARTICLE; CHEMISTRY; CLASSIFICATION; CLOSTRIDIUM; CRYSTALLIZATION; HYDROGEN BOND; MACROMOLECULE; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING;

BACTERIAL PROTEINS; CLOSTRIDIUM; CRYSTALLIZATION; HYDROGEN; HYDROGEN BONDING; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; NITROGEN ISOTOPES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; RUBREDOXINS;

EID: 0034167156     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2049     Document Type: Editorial

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