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1pef
From Proteopedia
(New page: 200px<br /><applet load="1pef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pef, resolution 1.5Å" /> '''PEPTIDE F (EQLLKALEFL...) |
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| - | [[Image:1pef.jpg|left|200px]]<br /><applet load="1pef" size=" | + | [[Image:1pef.jpg|left|200px]]<br /><applet load="1pef" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pef, resolution 1.5Å" /> | caption="1pef, resolution 1.5Å" /> | ||
'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''<br /> | '''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray diffraction analysis at 1.5 A resolution has confirmed the helical | + | 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== | ==About this Structure== | ||
| - | 1PEF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1PEF is a [http://en.wikipedia.org/wiki/Protein_complex 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8868477 8868477] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Garavito, R | + | [[Category: Garavito, R M.]] |
[[Category: Taylor, K.]] | [[Category: Taylor, K.]] | ||
| - | [[Category: Yang, N | + | [[Category: Yang, N C.]] |
[[Category: alpha-helical bundle]] | [[Category: alpha-helical bundle]] | ||
[[Category: synthetic protein]] | [[Category: synthetic protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:56 2008'' |
Revision as of 12:28, 21 February 2008
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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 Feb 21 14:27:56 2008
