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A proton nuclear magnetic resonance study of the conformation of bovine anaphylatoxin C5a in solution
Author(s) -
Zarbock Jutta,
Gennaro Renato,
Romeo Domenico,
Clore G.Marius,
Gronenborn Angela M.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80499-x
Subject(s) - chemistry , nuclear overhauser effect , nuclear magnetic resonance spectroscopy , crystallography , nuclear magnetic resonance , anaphylatoxin , amide , globular protein , two dimensional nuclear magnetic resonance spectroscopy , proton , spectroscopy , stereochemistry , biochemistry , physics , antibody , quantum mechanics , complement system , immunology , biology
The solution conformation of bovine anaphylatoxin C5a has been investigated by nuclear magnetic resonance (NMR) spectroscopy. The 1 H‐NMR spectrum is assigned in a sequential manner using a variety of two‐dimensional NMR techniques. A qualitative interpretation of the short range nuclear Overhauser enhancement data involving the NH, C α H and C β H protons suggests that C5a has four helices comprising residues 5–11, 15–25, 33–39 and 46–61, and is composed of a globular head (residues 5–61) and a C‐terminal tail. The polypeptide fold was determined by hybrid distance geometry‐dynamical simulated annealing calculations on the basis of 203 approximate interproton distance restraints, 22 distance restraints for 11 intrahelical hydrogen bonds (identified on the basis of the pattern of short range NOEs and slowly exchanging backbone amide protons) and restraints for the 3 disulfide bridges. The overall polypeptide fold is similar to that of the sequence related human recombinant anaphylatoxin C5a [(1988) Proteins 3, 139–145].