Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids

Journal of the American Chemical Society

Volumn 126, Issue 34, 2004, Pages 10560-10570

  Miclet, Emeric ^a   Williams Jr , David C ^a   Clore, G Marius ^a   Bryce, David L ^a   Boisbouvier, Jérôme ^a,b   Bax, Ad ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; DNA; HYDROGEN; MAGNETIC FIELDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RELAXATION PROCESSES;

CHEMICAL SHIFT ANISOTROPY; DIPOLAR INTERACTIONS; METHYLENE GROUPS; RELAXATION PROPERTIES;

PROTEINS;

BACTERIAL PROTEIN; CALMODULIN; CARBENE; DNA; HYDROGEN; IMMUNOGLOBULIN G; NUCLEIC ACID; PEPTIDE; PROTEIN; STREPTOCOCCAL PROTEIN G; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; BINDING SITE; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL BOND; CHEMICAL INTERACTION; DIPOLE; DYNAMICS; EVALUATION; MAGNETIC FIELD; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE ANALYSIS; RELAXATION TIME; SENSITIVITY AND SPECIFICITY; STRUCTURE ANALYSIS; TECHNIQUE;

DNA; HYDROCARBONS; METHANE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEIC ACID CONFORMATION; PROTEINS;

EID: 4344565815     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja047904v     Document Type: Article

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