Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution
- Stanford Univ. Medical School, CA (USA)
- National Research Council of Canada, Montreal, Quebec (Canada) Cornell Univ., Ithaca, NY (USA)
- Cornell Univ., Ithaca, NY (USA)
Proton NMR assignments have been made for 121 of the 124 residues of bovine pancreatic ribonuclease A (RNase A). During the first stage of assignment, COSY and relayed COSY data were used to identify 40 amino acid spin systems belonging to alanine, valine, threonine, isoleucine, and serine residues. Approximately 60 other NH-{alpha}CH-{beta}CH systems were also identified but not assigned to specific amino acid type. NOESY data then were used to connect sequentially neighboring spin systems; approximately 475 of the possible 700 resonances in RNase A were assigned in this way. The authors' assignments agree with those for 20 residues assigned previously. NOESY correlations were used to identify regular backbone structure elements in RNase A, which are very similar to those observed in X-ray crystallographic studies.
- OSTI ID:
- 5083281
- Journal Information:
- Biochemistry; (USA), Vol. 28:14; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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RNA-ASE
NUCLEAR MAGNETIC RESONANCE
AQUEOUS SOLUTIONS
CATTLE
CHEMICAL SHIFT
LEUCINE
OVERHAUSER EFFECT
PANCREAS
PROTONS
SERINE
THREONINE
VALINE
X-RAY DIFFRACTION
AMINO ACIDS
ANIMALS
BARYONS
BODY
CARBOXYLIC ACIDS
COHERENT SCATTERING
DIFFRACTION
DIGESTIVE SYSTEM
DISPERSIONS
DOMESTIC ANIMALS
ELEMENTARY PARTICLES
ENDOCRINE GLANDS
ENZYMES
ESTERASES
FERMIONS
GLANDS
HADRONS
HYDROLASES
HYDROXY ACIDS
MAGNETIC RESONANCE
MAMMALS
MIXTURES
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PHOSPHODIESTERASES
RESONANCE
RUMINANTS
SCATTERING
SOLUTIONS
VERTEBRATES
550601* - Medicine- Unsealed Radionuclides in Diagnostics