1pef

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[[Image:1pef.jpg|left|200px]]
[[Image:1pef.jpg|left|200px]]
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{{Structure
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|PDB= 1pef |SIZE=350|CAPTION= <scene name='initialview01'>1pef</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1pef", creates the "Structure Box" on the page.
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{{STRUCTURE_1pef| PDB=1pef | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pef OCA], [http://www.ebi.ac.uk/pdbsum/1pef PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pef RCSB]</span>
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'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
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==About this Structure==
==About this Structure==
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1PEF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA].
==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/8868477 8868477]
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:[http://www.ncbi.nlm.nih.gov/pubmed/8868477 8868477]
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[[Category: Protein complex]]
 
[[Category: Garavito, R M.]]
[[Category: Garavito, R M.]]
[[Category: Taylor, K.]]
[[Category: Taylor, K.]]
[[Category: Yang, N C.]]
[[Category: Yang, N C.]]
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[[Category: alpha-helical bundle]]
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[[Category: Alpha-helical bundle]]
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[[Category: synthetic protein]]
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[[Category: Synthetic protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:59:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:40 2008''
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Revision as of 01:59, 3 May 2008

Template:STRUCTURE 1pef

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

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 Sat May 3 04:59:38 2008

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