sup 1 H assignments and secondary structure determination of the soybean trypsin/chymotrypsin Bowman-Birk inhibitor

Journal Article · Tue Apr 09 00:00:00 EDT 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00228a002· OSTI ID:5509298

Werner, M H; Wemmer, D E ^[1]

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1. Univ. of California, Berkeley (USA)

The {sup 1}H resonance assignments and secondary structure of the trypsin/chymotrypsin Bowman-Birk inhibitor from soybeans were determined by nuclear magnetic resonance spectroscopy (NMR) at 600 MHz in an 18% acetonitrile-d{sub 3}/aqueous cosolvent. Resonances from 69 to 71 amino acids were assigned sequence specifically. Residues Q11-T15 form an antiparallel {beta}-sheet with residues Q21-S25 in the tryptic inhibitory domain and an analogous region of antiparallel sheet forms between residues S38-A42 and Q48-V52 in the chymotryptic inhibitory domain. The inhibitory sites of each fragment (K16-S17 for trypsin, L43-S44 for chymotrypsin) are each part of a type VI like turn at one end of their respective region of the antiparallel {beta}-sheet. These structural elements are compared to those found in other Bowman-Birk inhibitors.

• DOE Contract Number: AC03-76SF00098; FG05-86ER75281
• OSTI ID: 5509298
• Journal Information: Biochemistry; (United States), Vol. 30:14; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
ENZYME INHIBITORS
NUCLEAR MAGNETIC RESONANCE
AMINO ACID SEQUENCE
CHYMOTRYPSIN
MOLECULAR STRUCTURE
PROTONS
SERINE PROTEINASES
SOYBEANS
TRYPSIN
BARYONS
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
FOOD
HADRONS
HYDROLASES
MAGNETIC RESONANCE
NUCLEONS
PEPTIDE HYDROLASES
PLANTS
RESONANCE
VEGETABLES
550601* - Medicine- Unsealed Radionuclides in Diagnostics