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Article

Aromatic cluster mutations produce focal modulations of β-sheet structure.

Protein science : a publication of the Protein Society - 1 May 2015

Biancalana Matthew, Makabe Koki, Yan Shude, Koide Shohei

Abstract excerpt

Site-directed mutagenesis is a powerful tool for altering the structure and function of proteins in a focused manner. Here, we examined how a model β-sheet protein could be tuned by mutation of numerous surface-exposed residues to aromatic amino acids. We designed these aromatic side chain "clusters" at highly solvent-exposed positions in the flat, single-layer β-sheet of Borrelia outer surface protein A (OspA)....

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Share to Amino Acids, Aromatic
Share to Antigens, Surface
Share to Bacterial Outer Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Crystallography, X-Ray

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Share to Protein Structure, Secondary

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Identifiers

PMID: 25645104
DOI: 10.1002/pro.2657
PMCID: PMC4420532

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