Publication

Engineering of zinc finger and MHC motifs to locked-in tertiary folds

1997
Journal Articles

Abstract

The assembly of helical and b-sheet peptide blocks contg. reactive chain ends results in highly branched chain architectures ("locked-in folds") mimicking native tertiary structures. This mol. kit strategy allows to bypass the protein folding problem in protein de novo design and gives access to protein mimetics of high thermo-dynamic stability. The validity of this concept is exemplified for the design and synthesis of locked-in folds mimicking the zinc finger and MHC folding motifs. [on SciFinder (R)]

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1997
Journal Articles

Abstract

Official source

Related concepts (17)

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Protein design

Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. Proteins can be designed from scratch (de novo design) or by making calculated variants of a known protein structure and its sequence (termed protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to specific structures.

Protein fold class

In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). Four large classes of protein that are generally agreed upon by the two main structure classification databases (SCOP and CATH).

Related publications (17)

Engineering of zinc finger and MHC motifs to locked-in tertiary folds

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