Venkatraman, Janani and Shankaramma, Sasalu C and Balaram, Padmanabhan (2001) Design of Folded Peptides. In: Chemical Reviews, 101 (10). pp. 3131-3152.
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The construction of complex protein folds relies on the precise conversion of a linear polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link sequence and folding is intricate and yet to be firmly elucidated. Examination of protein 3-dimensional structures suggests that complex tertiary folds and quaternary associations can be deconstructed into a limited number of secondary structural elements, such as strands, helices, and turns, which are assembled using loosely structured loops (Figure 1). The stability of a specific fold is determined by tertiary interactions between residues which are distant in sequence. De novo design of existing or novel protein folds demands a thorough understanding of the rules that underlie protein structure and stability.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to American Chemical Society|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||20 Aug 2004|
|Last Modified:||19 Sep 2010 04:14|
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