Natural selection, protein engineering, and the last riboorganism: Rational model building in biochemistry

Benner, S. A., Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830, Ellington, A. D, Ge, L., Glasfeld, A., Leanz, G. F., Krauch, T., MacPeherson, L. J., Moroney, S., Piccirilli, J. A. and Weinhold, E. 1987. Natural selection, protein engineering, and the last riboorganism: Rational model building in biochemistry. Evolution of Catalytic Function, CSH Symposia on Quantitative Biology, vol. 52. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, pp. 53-63. (10.1101/sqb.1987.052.01.009)

Full text not available from this repository.

Abstract

The behavior of biological macromolecules can be interpreted both functionally and historically (Benner et al. 1985). Functional interpretations presume natural selection and require a distinction between macromolecular behaviors that are the products of selection and those that reflect neutral drift. Historical interpretations require distinctions between “primitive traits” present in a common ancestor and “derived” traits that arose more recently. These distinctions are extremely difficult to make. Therefore, appropriate research strategy involves construction of formal models that can be set in opposition to each other and experimentally tested. The building and testing of historical and functional models are described in this paper. We hope to illustrate how rigorous model building can (1) help distinguish between selected and nonselected behaviors in proteins, (2) permit the engineering of the catalytic properties of enzymes, and (3) define the role of RNA in early catalysis.

Item Type:	Book Section
Date Type:	Publication
Status:	Published
Schools:	Research Institutes & Centres > Cardiff Catalysis Institute (CCI) Schools > Chemistry
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Publisher:	Cold Spring Harbor Laboratory
ISBN:	0879690542
Last Modified:	17 Oct 2025 15:51
URI:	https://orca.cardiff.ac.uk/id/eprint/14282

Citation Data

Cited 64 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item