1abz
From Proteopedia
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| - | [[Image:1abz.gif|left|200px]] | + | [[Image:1abz.gif|left|200px]] |
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| - | '''ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1abz |SIZE=350|CAPTION= <scene name='initialview01'>1abz</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ABZ is a [ | + | 1ABZ 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=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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/9300486 9300486] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Connolly, P J.]] | [[Category: Connolly, P J.]] | ||
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[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''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 09:55:38 2008'' |
Revision as of 07:55, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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 Mar 20 09:55:38 2008
