1pef
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(New page: 200px<br /><applet load="1pef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pef, resolution 1.5Å" /> '''PEPTIDE F (EQLLKALEFL...)
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Revision as of 00:15, 25 November 2007
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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
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