Preferred conformational state of the N‐terminus section of a bovine growth hormone fragment (residues 96‐133) in water is an omega loop

Abstract

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. Copyright © 1988 Alan R. Liss, Inc.