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Preferred conformational state of the N‐terminus section of a bovine growth hormone fragment (residues 96‐133) in water is an omega loop
Author(s) -
Gooley P. R.,
Carter S. A.,
Fagerness P. E.,
MacKenzie N. E.
Publication year - 1988
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340040107
Subject(s) - residue (chemistry) , amino acid residue , omega , nuclear overhauser effect , loop (graph theory) , chemistry , fragment (logic) , bovine somatotropin , stereochemistry , protein secondary structure , crystallography , peptide sequence , hormone , growth hormone , nuclear magnetic resonance spectroscopy , physics , biochemistry , mathematics , algorithm , combinatorics , quantum mechanics , gene
The solution structure of a 38‐amino‐acid‐residue, biologically active fragment of bovine growth hormone (bGH96–133) was investigated with a combined nuclear magnetic resonance (NMR) and computer modeling approach. With the distance geometry program DISGEO and distance constraints derived from the nuclear Overhauser enhancement (NOE) experiments, it was found that residues Ser‐100 to Tyr‐110 circumscribe an Ω‐loop, a recently categorized feature of nonregular secondary protein structure.