1pef: Difference between revisions

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[[Image:1pef.jpg|left|200px]]
{{Seed}}
[[Image:1pef.png|left|200px]]


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{{STRUCTURE_1pef|  PDB=1pef  |  SCENE=  }}  
{{STRUCTURE_1pef|  PDB=1pef  |  SCENE=  }}  


'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
===PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_8868477}}, adds the Publication Abstract to the page
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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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:59:38 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:19:33 2008''

Revision as of 09:19, 27 July 2008

File: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

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