Sequence and structural analysis of two designed proteins with 88% identity adopting different folds
نویسندگان
چکیده
منابع مشابه
Sequence and structural analysis of two designed proteins with 88% identity adopting different folds.
Protein folding is a natural phenomenon by which a sequence of amino acids folds into a unique functional three-dimensional structure. Although the sequence code that governs folding remains a mystery, one can identify key inter-residue contacts responsible for a given topology. In nature, there are many pairs of proteins of a given length that share little or no sequence identity. Similarly, t...
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How protein sequence codes for 3D structure remains a fundamental question in biology. One approach to understanding the folding code is to design a pair of proteins with maximal sequence identity but retaining different folds. Therefore, the nonidentities must be responsible for determining which fold topology prevails and constitute a fold-specific folding code. We recently designed two prote...
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Proteins that share common ancestry may differ in structure and function because of divergent evolution of their amino acid sequences. For a typical diverse protein superfamily, the properties of a few scattered members are known from experiment. A satisfying picture of functional and structural evolution in relation to sequence changes, however, may require characterization of a larger, well c...
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15 صفحه اولwoman-defined identity: analysis of selected poems of adrienne rich
the current thesis is composed in five chapters in the following fashion: chapter two encompasses the applied framework of the project in details; the methodology of carl gustav jung to explain the process of individuation, the major archetypes and their attributes and his techniques to assess the mind’s strata are all explained. moreover, the austrian psychoanalysts, heinz kohut’s models of a...
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ژورنال
عنوان ژورنال: Protein Engineering Design and Selection
سال: 2010
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/gzq070