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1pef

From Proteopedia

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{{STRUCTURE_1pef| PDB=1pef | SCENE= }}
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'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
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===PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 8868477 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8868477}}
==About this Structure==
==About this Structure==
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[[Category: Alpha-helical bundle]]
[[Category: Alpha-helical bundle]]
[[Category: Synthetic protein]]
[[Category: Synthetic protein]]
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Revision as of 09:19, 27 July 2008

Image:1pef.png

Template:STRUCTURE 1pef

PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE

Template:ABSTRACT PUBMED 8868477

About this Structure

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 Sun Jul 27 12:19:33 2008

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