1pef
From Proteopedia
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| - | [[Image:1pef.jpg|left|200px]] | + | [[Image:1pef.jpg|left|200px]] |
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| - | '''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE''' | + | {{Structure |
| + | |PDB= 1pef |SIZE=350|CAPTION= <scene name='initialview01'>1pef</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PEF is a [ | + | 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]. |
==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:// | + | 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] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Garavito, R M.]] | [[Category: Garavito, R M.]] | ||
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[[Category: synthetic protein]] | [[Category: synthetic protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:23:19 2008'' |
Revision as of 11:23, 20 March 2008
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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
