Chemical ligation and isotope labeling to locate dynamic effects

Scott, Alan F., Luk, Louis Yu Pan ORCID: https://orcid.org/0000-0002-7864-6261 and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 2017. Chemical ligation and isotope labeling to locate dynamic effects. Imperiali, Barbara, ed. Methods in Enzymology, Vol. 596. Elsevier, pp. 23-41. (10.1016/bs.mie.2017.06.040)

Full text not available from this repository.

Abstract

Heavy isotope labeling of enzymes slows protein motions without disturbing the electrostatics and can therefore be used to probe the role of dynamics in enzyme catalysis. To identify the structural elements responsible for dynamic effects, individual segments of an enzyme can be labeled and the resulting effect on the kinetics of the reaction can be measured. Such hybrid isotopomers can be constructed by expressed protein ligation, in which complementary labeled and unlabeled peptide segments are prepared by recombinant gene expression and linked by means of chemical ligation. The construction of such hybrid isotopomers is exemplified here with the paradigmatic enzyme dihydrofolate reductase (DHFR) from Escherichia coli.

Item Type:	Book Section
Date Type:	Published Online
Status:	Published
Schools:	Chemistry
Publisher:	Elsevier
ISBN:	9780128114698
ISSN:	0076-6879
Last Modified:	03 Nov 2022 10:10
URI:	https://orca.cardiff.ac.uk/id/eprint/107155

Citation Data

Cited 2 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item