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. 1996 Mar;5(3):414–421. doi: 10.1002/pro.5560050302

A novel, multilayer structure of a helical peptide.

K S Taylor 1, M Z Lou 1, T M Chin 1, N C Yang 1, R M Garavito 1
PMCID: PMC2143371  PMID: 8868477

Abstract

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.

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Selected References

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