262l

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File:262l.png

Template:STRUCTURE 262l

STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDINGSTRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING

Template:ABSTRACT PUBMED 10339544

About this StructureAbout this Structure

262L is a 2 chains structure of sequences from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Sagermann M, Baase WA, Matthews BW. Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding. Proc Natl Acad Sci U S A. 1999 May 25;96(11):6078-83. PMID:10339544

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OCA

[1] Sagermann M, Baase WA, Matthews BW. Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding. Proc Natl Acad Sci U S A. 1999 May 25;96(11):6078-83. PMID:10339544

[xtra 1]