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| - | [[Image:1fme.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1fme| PDB=1fme | SCENE= }} | | {{STRUCTURE_1fme| PDB=1fme | SCENE= }} |
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| - | '''SOLUTION STRUCTURE OF FSD-EY, A NOVEL PEPTIDE ASSUMING A BETA-BETA-ALPHA FOLD'''
| + | ===SOLUTION STRUCTURE OF FSD-EY, A NOVEL PEPTIDE ASSUMING A BETA-BETA-ALPHA FOLD=== |
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| - | ==Overview==
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| - | The computational redesign of the second zinc finger of Zif268 to produce a 28 residue peptide (FSD-1) that assumes a betabetaalpha fold without metal binding was recently reported. In order to explore the tolerance of this metal-free fold towards sequence variability, six additional peptides resulting from the ORBIT computational protein design process were synthesized and characterized. The experimental stabilities of five of these peptides are strongly correlated with the energies calculated by ORBIT. However, when a peptide with a mutation in the beta-turn is examined, the calculated stability does not accurately predict the experimentally determined stability. The NMR solution structure of a peptide incorporating this mutation (FSD-EY) reveals that the register between the beta-strands is different from the model structure used to select and score the sequences. FSD-EY has a type I' turn instead of the target EbaaagbE turn (rubredoxin knuckle). Two additional peptides that have improved side-chain to backbone hydrogen bonding and turn propensity for the target turn were characterized. Both are of stability comparable to that of FSD-1. These results demonstrate the robustness of the ORBIT protein design methods and underscore the need for continued improvements in negative design. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11292351}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11292351 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11292351}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FME OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FME OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Fsd-1]] | | [[Category: Fsd-1]] |
| | [[Category: Zinc finger]] | | [[Category: Zinc finger]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:30:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:29:02 2008'' |
Revision as of 00:29, 1 July 2008
Template:STRUCTURE 1fme
SOLUTION STRUCTURE OF FSD-EY, A NOVEL PEPTIDE ASSUMING A BETA-BETA-ALPHA FOLD
Template:ABSTRACT PUBMED 11292351
About this Structure
Full experimental information is available from OCA.
Reference
The beta-beta-alpha fold: explorations in sequence space., Sarisky CA, Mayo SL, J Mol Biol. 2001 Apr 13;307(5):1411-8. PMID:11292351
Page seeded by OCA on Tue Jul 1 03:29:02 2008
