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American Chemical Society, Biomacromolecules, 11(11), p. 3216-3218, 2010

DOI: 10.1021/bm100965y

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Chain stiffness of elastin-like polypeptides

Journal article published in 2010 by Sabine Fluegel, Karl Fischer, Jonathan R. McDaniel ORCID, Ashutosh Chilkoti, Manfred Schmidt
This paper is available in a repository.
This paper is available in a repository.

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Abstract

The hydrodynamic radii of a series of genetically engineered monodisperse elastin like polypeptides (ELP) was determined by dynamic light scattering in aqueous solution as function of molar mass. Utilizing the known theoretical expression for the hydrodynamic radius of wormlike chains, the Kuhn statistical segment length was determined to be lk = 2.1 nm, assuming that the length of the peptide repeat unit was b = 0.365 nm, a value derived for a coiled conformation of ELP. The resulting chain stiffness is significantly larger than previously reported by force-distance curve analysis (lk