1pef: Difference between revisions

Line 1:

[[Image:1pef.jpg|left|200px]]<br /><applet load="1pef" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pef.jpg|left|200px]]<br /><applet load="1pef" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pef, resolution 1.5Å" />

'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA].

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==

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: Garavito, R.M.]]

[[Category: Garavito, R M.]]

[[Category: Taylor, K.]]

[[Category: Yang, N.C.]]

[[Category: Yang, N C.]]

[[Category: alpha-helical bundle]]

[[Category: synthetic protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 25 02~~:23:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:56 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1pef.jpg|left|200px]]<br /><applet load="1pef" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pef.jpg|left|200px]]<br /><applet load="1pef" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pef, resolution 1.5&Aring;" />
 '''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''<br />
 ==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.
+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==
-PEF 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA].
+PEF 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==
 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: Garavito, R.M.]]
+[[Category: Garavito, R M.]]
 [[Category: Taylor, K.]]
-[[Category: Yang, N.C.]]
+[[Category: Yang, N C.]]
 [[Category: alpha-helical bundle]]
 [[Category: synthetic protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:23:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:56 2008''