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2avp
From Proteopedia
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Crystal structure of an 8 repeat consensus TPR superhelix
Overview
The folding/unfolding transitions of a series of designed consensus tetratricopeptide repeat proteins are quantitatively described by the classical one-dimensional Ising model, which thus represents a new folding paradigm for repeat proteins. Moreover, for the first time for any protein, a theoretical model predicts the folding/unfolding transition midpoint and the width of the transition.
About this Structure
2AVP is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
A new folding paradigm for repeat proteins., Kajander T, Cortajarena AL, Main ER, Mochrie SG, Regan L, J Am Chem Soc. 2005 Jul 27;127(29):10188-90. PMID:16028928
Page seeded by OCA on Thu Feb 21 16:31:28 2008
