Year: 1996
Type: article
Abstract: The successful design of proteins requires careful consideration of the multiplicity of forces that stabilize their three-dimensional structures including hydrophobic interactions, hydrogen-bonding, electrostatics and weakly polar interactions. Early attempts to design proteins relied too heavily on hydrophobic interactions to provide stability, resulting in structures with dynamic properties. Addition of more specific interactions to these initial designs gives rise to proteins with more native-like properties. This manuscript describes the design of native-like three- and four-helix bundles, and their cloning and expression of these proteins.
Authors: S. F. Betz, J. W. Bryson, M. C. Passador, R. J. Brown, K. T. O'Neil, W. F. DeGrado, Kjell Undheim, Connie N. Rosendahl, Monika Haugg, Nathalie Trabesinger-Rüf, Elmar G. Weinhold
Institution: DuPont (United States)
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
OpenAlex ID: W2953145992