Srinivas, G and Bagchi, B (2002) Folding and unfolding of chicken villin headpiece: Energy landscape of a single-domain model protein. In: Current Science, 82 (2). pp. 179-185.
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Folding and unfolding of a thermostable chicken villin headpiece subdomain, a 36-residue protein (HP-36), is studied by using Brownian dynamics simulations. The hydropathy scale of amino acids is used to obtain the varying interactions among the amino acids. A qualitative picture of the energy landscape funnel is obtained from simulations. Although there are several states near the minimum of the folding funnel, we could identify a stable native configuration. The energy of the folded protein scales with the hydrophobic contact parameter, as found in recent analyses. The model also allows for a description of cold denaturation by the salt-induced modification of the 'effective' interactions among the various amino acids. In this model, the kinetics of denaturation is found to be considerably different from that of folding-folding, seems to face more barriers and involves a more complex pathway.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Indian Academy of Sciences.|
|Department/Centre:||Division of Chemical Sciences > Solid State & Structural Chemistry Unit|
|Date Deposited:||02 Jun 2006|
|Last Modified:||19 Sep 2010 04:28|
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