1abz

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[[Image:1abz.png|left|200px]]
 
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{{STRUCTURE_1abz| PDB=1abz | SCENE= }}
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==ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES==
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<StructureSection load='1abz' size='340' side='right'caption='[[1abz]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1abz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ABZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1abz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abz OCA], [https://pdbe.org/1abz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1abz RCSB], [https://www.ebi.ac.uk/pdbsum/1abz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1abz ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES===
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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<ref>PMID:9300486</ref>
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{{ABSTRACT_PUBMED_9300486}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1abz" style="background-color:#fffaf0;"></div>
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[[1abz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABZ OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:009300486</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Connolly, P J.]]
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[[Category: Large Structures]]
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[[Category: Fezoui, Y.]]
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[[Category: Connolly PJ]]
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[[Category: Osterhout, J J.]]
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[[Category: Fezoui Y]]
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[[Category: De novo design]]
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[[Category: Osterhout JJ]]
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[[Category: Helix-turn-helix]]
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ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES

PDB ID 1abz

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