1pef
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1pef.jpg|left|200px]] | [[Image:1pef.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1pef", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1pef| PDB=1pef | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE''' | '''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | + | 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] | ||
| - | [[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.]] | ||
| - | [[Category: | + | [[Category: Alpha-helical bundle]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 01:59, 3 May 2008
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
