Biochemistry & Analytical Biochemistry

Michael Blaber

Publications

• Clinical image
  An Efficiently-folding Purely-symmetric de novo Designed Protein
  Author(s): Michael BlaberMichael Blaber
  
  Many globular protein folds exhibit some form of rotational symmetry – the most common example being the TIM barrel (having 8-fold rotational symmetry of a repeating beta-strand/turn/alpha- helix/turn motif). This type of common symmetry in proteins was apparent from the earliest days of X-ray structure studies, leading to the hypothesis that gene duplication and fusion was the underlying evolutionary mechanism. However, while such symmetry at the 3°- structure level is apparent, any 1°-structure symmetry when comparing repeating structural motifs is often largely absent. Such sequence analyses, along with theoretical considerations of folding frustration for exact repeating motifs, as well as natively-unstructured properties for peptides having reduced sequence complexity (as occurs with exact repeating motifs), resulted in a paradigm .. View More»
  DOI: 10.4172/2161-1009.1000i104

  Abstract PDF