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1pef
From Proteopedia
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| , resolution 1.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE
Overview
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.
About this Structure
1PEF is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:23:19 2008
