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Please use this identifier to cite or link to this item: http://dspace.lib.cranfield.ac.uk/handle/1826/2536

Document Type: Article
Title: On adsorption-induced denaturation of folded proteins.
Authors: Fernández, Ariel
Ramsden, Jeremy J.
Issue Date: Dec-2001
Citation: Ariel Fernández and Jeremy J. Ramsden; On adsorption-induced denaturation of folded proteins. Journal of Biological Physics and Chemistry Vol 1 No 2, 2001 pp81–84
Abstract: In the absence of intramolecular long range interactions, the extended local conformation of a peptide chain is entropically favoured over compact ones, since the area of the Ramachandran basin of attraction is larger for the extended local conformation than for any other. In consequence, a random coil is predominantly in the extended conformation. Under refolding conditions, the high entropic content of the random coil is countered by the enthalpy loss associated with intramolecular contact formation (“hydrophobic collapse”) and compactification of the chain. At an appropriate protein-binding surface, however, the enthalpy loss can be achieved at minimal cost of conformational entropy, since contacts can be formed between the protein and the surface and hence do not require compactification of the protein chain. This saving in entropic cost is a central concept for understanding the surface-induced denaturation of folded proteins.
URI: http://hdl.handle.net/1826/2536
Appears in Collections:Staff publications - School of Applied Sciences

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