1abz
From Proteopedia
(New page: 200px<br /><applet load="1abz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1abz" /> '''ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, N...) |
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| - | [[Image:1abz.gif|left|200px]]<br /><applet load="1abz" size=" | + | [[Image:1abz.gif|left|200px]]<br /><applet load="1abz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1abz" /> | caption="1abz" /> | ||
'''ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES'''<br /> | '''ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | alpha t alpha is a 38-residue peptide designed to adopt a helical hairpin | + | alpha t alpha is a 38-residue peptide designed to adopt a helical hairpin conformation in solution (Fezoui Y, Weaver DL Osterhout JJ, 1995, Protein Sci 4:286-295). A previous study of the carboxylate form of alpha t alpha by CD and two-dimensional NMR indicated that the peptide was highly helical and that the helices associated in approximately the intended orientation (Fezoui Y, Weaver DL, Osterhout JJ, 1994, Proc Natl Acad Sci USA 91:3675-3679). Here, the solution structure of alpha t alpha as determined by two-dimensional NMR is reported. A total of 266 experimentally derived distance restraints and 20 dihedral angle restraints derived from J-couplings were used. One-hundred initial structures were generated by distance geometry and refined by dynamical simulated annealing. Twenty-three of the lowest-energy structures consistent with the experimental restraints were analyzed. The results presented here show that alpha t alpha is comprised of two associating helices connected by a turn region. |
==About this Structure== | ==About this Structure== | ||
| - | 1ABZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ABZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABZ OCA]. |
==Reference== | ==Reference== | ||
Solution structure of alpha t alpha, a helical hairpin peptide of de novo design., Fezoui Y, Connolly PJ, Osterhout JJ, Protein Sci. 1997 Sep;6(9):1869-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9300486 9300486] | Solution structure of alpha t alpha, a helical hairpin peptide of de novo design., Fezoui Y, Connolly PJ, Osterhout JJ, Protein Sci. 1997 Sep;6(9):1869-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9300486 9300486] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Connolly, P | + | [[Category: Connolly, P J.]] |
[[Category: Fezoui, Y.]] | [[Category: Fezoui, Y.]] | ||
| - | [[Category: Osterhout, J | + | [[Category: Osterhout, J J.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: de novo design]] | [[Category: de novo design]] | ||
| Line 20: | Line 20: | ||
[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:56 2008'' |
Revision as of 09:42, 21 February 2008
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ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES
Overview
alpha t alpha is a 38-residue peptide designed to adopt a helical hairpin conformation in solution (Fezoui Y, Weaver DL Osterhout JJ, 1995, Protein Sci 4:286-295). A previous study of the carboxylate form of alpha t alpha by CD and two-dimensional NMR indicated that the peptide was highly helical and that the helices associated in approximately the intended orientation (Fezoui Y, Weaver DL, Osterhout JJ, 1994, Proc Natl Acad Sci USA 91:3675-3679). Here, the solution structure of alpha t alpha as determined by two-dimensional NMR is reported. A total of 266 experimentally derived distance restraints and 20 dihedral angle restraints derived from J-couplings were used. One-hundred initial structures were generated by distance geometry and refined by dynamical simulated annealing. Twenty-three of the lowest-energy structures consistent with the experimental restraints were analyzed. The results presented here show that alpha t alpha is comprised of two associating helices connected by a turn region.
About this Structure
1ABZ is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of alpha t alpha, a helical hairpin peptide of de novo design., Fezoui Y, Connolly PJ, Osterhout JJ, Protein Sci. 1997 Sep;6(9):1869-77. PMID:9300486
Page seeded by OCA on Thu Feb 21 11:42:56 2008
