Two-dimensional NMR studies of Kazal proteinase inhibitors. 1. Sequence-specific assignments and secondary structure of turkey ovomucoid third domain
Two-dimensional proton NMR experiments have been used to sequentially assign resonances to all of the peptide backbone protons of turkey ovomucoid third domains (OMTKY3) except those of the N-terminal ..cap alpha..-amino group whose signal was not resolved owing to exchange with the solvent. Assignments also have been made for more than 80% of the side-chain protons. Two-dimensional chemical shift correlated spectroscopy (COSY), relayed coherence transfer spectroscopy (RELAY), and two-dimensional homonuclear Hartmann-Hahn spectroscopy (HOHAHA) were used to identify the spin systems of almost half of the residues prior to sequential assignment. Assignments were based on two-dimensional nuclear Overhauser enhancements observed between adjacent resides. The secondary structure of OMTKY3 in solution was determined from additional assigned NOESY cross-peaks; it closely resembles the secondary structure determined by single-crystal X-ray diffraction of OMTKY3 in complex with Streptomyces griseus proteinase B. The NMR data provide evidence for three slowly exchanging amide protons that were not identified as hydrogen-bond donors in the crystal structure.
- Research Organization:
- Univ. of Wisconsin, Madison (USA)
- OSTI ID:
- 5238041
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:7; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
62 RADIOLOGY AND NUCLEAR MEDICINE
AMINO ACID SEQUENCE
ANIMALS
BACTERIA
BIRDS
CARBOHYDRATES
CHEMICAL BONDS
CHEMICAL SHIFT
COHERENT SCATTERING
DEUTERIUM COMPOUNDS
DIFFRACTION
ENZYME INHIBITORS
ENZYMES
FOWL
GLUCOPROTEINS
HEAVY WATER
HYDROGEN COMPOUNDS
HYDROLASES
MAGNETIC RESONANCE
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
OXYGEN COMPOUNDS
PEPTIDE HYDROLASES
PROTEINS
RESONANCE
SACCHARIDES
SCATTERING
STAPHYLOCOCCUS
VERTEBRATES
WATER
X-RAY DIFFRACTION