Ball, Robin and Fink, Thomas M. A. (2000) Kinetic capacity of a protein. Working Paper. Cornell: Cornell University Library.

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Abstract

The ability of a protein to recognise multiple independent target conformations was demonstrated in [1]. Here we consider the recognition of correlated configurations, which we apply to funnel design for a single conformation. The maximum basin of attraction, as parametrised in our model, depends on the number of amino acid species as ln A, independent of protein length. We argue that the extent to which the protein energy landscape can be manipulated is fixed, effecting a trade-off between well breadth, well depth and well number. This clarifies the scope and limits of protein and heteropolymer function.

Item Type:	Working or Discussion Paper (Working Paper)
Subjects:	Q Science > QC Physics
Divisions:	Faculty of Science > Physics
Library of Congress Subject Headings (LCSH):	Chemical kinetics, Proteins
Publisher:	Cornell University Library
Place of Publication:	Cornell
Official Date:	August 2000
Dates:	Date Event August 2000 Submitted
Number of Pages:	5
Status:	Not Peer Reviewed
Access rights to Published version:	Open Access

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