1pef

Publication Abstract from PubMed

X-ray diffraction analysis at 1.5 A resolution has confirmed the helical conformation of a de novo designed 18-residue peptide. However, the crystal structure reveals the formation of continuous molecular layers of parallel-packed amphiphilic helices as a result of much more extensive helix-helix interactions than predicted. The crystal packing arrangement, by virtue of distinct antiparallel packing interactions, segregates the polar and apolar surfaces of the helices into discrete and well-defined interfacial regions. An extensive "ridges-into-grooves" interdigitation characterizes the hydrophobic interface, whereas an extensive network of salt bridges and hydrogen bonds dominates the corresponding hydrophilic interface.

A novel, multilayer structure of a helical peptide.,Taylor KS, Lou MZ, Chin TM, Yang NC, Garavito RM Protein Sci. 1996 Mar;5(3):414-21. PMID:8868477^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.