1vqd: Difference between revisions
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{{STRUCTURE_1vqd| PDB=1vqd | SCENE= }} | |||
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'''GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)''' | '''GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)''' | ||
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[[Category: Skinner, M M.]] | [[Category: Skinner, M M.]] | ||
[[Category: Terwilliger, T C.]] | [[Category: Terwilliger, T C.]] | ||
[[Category: | [[Category: Dna-binding protein]] | ||
[[Category: | [[Category: Gene v]] | ||
[[Category: | [[Category: Mutant]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:47:39 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 12:47, 3 May 2008
GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)
OverviewOverview
The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.
About this StructureAbout this Structure
1VQD is a Single protein structure of sequence from Enterobacteria phage f1. Full crystallographic information is available from OCA.
ReferenceReference
Potential use of additivity of mutational effects in simplifying protein engineering., Skinner MM, Terwilliger TC, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:8855252 Page seeded by OCA on Sat May 3 12:47:39 2008