><Publications

Rapporti ISTISAN – Proceedings of the International meeting "Complexity in the living: a problem-oriented approach", Rome, 2004, 05/20, 136–151 (2005)

Aggregation propensity of proteins quantified by hydrophobicity

J. P. Zbilut, J. C. Mitchell, A. Giuliani, A. Colosimo, N. Marwan, M. Colafranceschi, C. L. Webber, Jr.

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(Introduction:) It has been well appreciated that the native state fold of proteins is in some way dependent upon the physico-chemical properties of their amino acid sequence, most notably, hydrophobicity. More recently it has been recognized that the actual folding process is of a stochastic nature, and also includes the possibility of forming aggregates that ultimately can be physiologically harmful. A growing body of evidence suggests that this involves partially or completely unfolded proteins. Yet, what factors specifically promote the formation of aggregates as opposed to native folds under relatively normal conditions remain undecided.

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