Sequence-specific sup 1 H NMR assignments and secondary structure of eglin c

Journal Article · Tue Feb 13 04:00:00 EST 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00458a018· OSTI ID:6896402

Hyberts, S G; Wagner, G ^[1]

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1. Univ. of Michigan, Ann Arbor (USA)

Sequence-specific nuclear magnetic resonance assignments were obtained for eglin c, a polypeptide inhibitor of the granulocytic proteinases elastase and cathepsin G and some other proteinases. The protein consists of a single polypeptide chain of 70 residues. All proton resonances were assigned except for some labile protons of arginine side chains. The patterns of nuclear Overhauser enhancements and coupling constants and the observation of slow hydrogen exchange were used to characterize the secondary structure of the protein. The results indicate that the solution structure of the free inhibitor is very similar to the crystal structure reported for the same protein in the complex with subtilisin Carlsberg. However, a part of the binding loop seems to have a significantly different conformation in the free protein.

• OSTI ID: 6896402
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:6; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ALANINES
AMINO ACIDS
ANIMALS
BARYONS
CARBOXYLIC ACIDS
CHEMICAL SHIFT
EGCR REACTOR
ELEMENTARY PARTICLES
ENRICHED URANIUM REACTORS
ENZYME INHIBITORS
ENZYMES
EXPERIMENTAL REACTORS
FERMIONS
GAS COOLED REACTORS
GLYCINE
GRAPHITE MODERATED REACTORS
HADRONS
HELIUM COOLED REACTORS
HYDROLASES
HYDROXY ACIDS
INHIBITION
INVERTEBRATES
LEUCINE
MAGNETIC RESONANCE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PEPTIDE HYDROLASES
PEPTIDES
POLYPEPTIDES
POWER REACTORS
PROTEINS
PROTONS
REACTORS
RESEARCH AND TEST REACTORS
RESONANCE
THERMAL REACTORS
THREONINE
VALINE