Hydrophobic models of protein folding and the thermodynamics of chain-boundary interactions

Please use this identifier to cite or link to this item: http://dspace.mediu.edu.my:8181/xmlui/handle/123456789/8222

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DC Field	Value	Language
dc.creator	Erzan Ayse	-
dc.creator	Tüzel Erkan	-
dc.date	2003	-
dc.date.accessioned	2013-06-01T10:34:04Z	-
dc.date.available	2013-06-01T10:34:04Z	-
dc.date.issued	2013-06-01	-
dc.identifier	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-97332003000300018	-
dc.identifier	http://www.doaj.org/doaj?func=openurl&genre=article&issn=01039733&date=2003&volume=33&issue=3&spage=573	-
dc.identifier.uri	http://koha.mediu.edu.my:8181/jspui/handle/123456789/8222	-
dc.description	We review some results concerning the energetic and dynamical consequences of taking a generic hydrophobic model of a random polypeptide chain, where the effective hydrophobic interactions are represented by Hookean springs. Then we present a set of calculations on a microscopic model of hydrophobic interactions, investigating the behaviour of a hydrophobic chain in the vicinity of a hydrophobic boundary. We conclude with some speculations as to the thermodynamics of pre-biotic functions proteins may have discharged very early on in the evolutionary past.	-
dc.publisher	Sociedade Brasileira de Física	-
dc.source	Brazilian Journal of Physics	-
dc.title	Hydrophobic models of protein folding and the thermodynamics of chain-boundary interactions	-
Appears in Collections:	Physics and Astronomy

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