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AbstractAbstract
[en] The thermal transition of bovine pancreatic ribonuclease A (RNase A) was investigated using proton nuclear magnetic resonance (NMR). Significant resonance overlap in the large native protein limits accurate assignments in the 1H NMR spectrum. This study proposes extending the investigation of large proteins by dynamic analysis. Comparison of the traditional method and the correlation coefficient method suggests successful application of spectrum image analysis in dynamic protein studies by NMR
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Journal Article
Journal
Tsinghua Science and Technology; ISSN 1007-0214; ; v. 6(3); p. 285-288
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ANIMALS, BARYONS, BODY, DIAGNOSTIC TECHNIQUES, DIGESTIVE SYSTEM, DOMESTIC ANIMALS, ELEMENTARY PARTICLES, ENDOCRINE GLANDS, ENTHALPY, ENZYMES, ESTERASES, EVALUATION, FERMIONS, FUNCTIONS, GLANDS, HADRONS, HYDROGEN ISOTOPES, HYDROLASES, ISOTOPES, LIGHT NUCLEI, MAGNETIC RESONANCE, MAMMALS, NUCLEASES, NUCLEI, NUCLEONS, ODD-EVEN NUCLEI, ORGANIC COMPOUNDS, ORGANS, PHOSPHODIESTERASES, PHYSICAL PROPERTIES, PROTEINS, RESONANCE, RUMINANTS, SPECTRA, STABLE ISOTOPES, THERMODYNAMIC PROPERTIES, VERTEBRATES
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