Streptavidin-biotin binding energetics.

Published

Journal Article (Review)

The high affinity energetics in the streptavidin-biotin system provide an excellent model system for studying how proteins balance enthalpic and entropic components to generate an impressive overall free energy for ligand binding. We review here concerted site-directed mutagenesis, biophysical, and computational studies of aromatic and hydrogen bonding interaction energetics between streptavidin and biotin. These results also have provided insight into how streptavidin builds a large activation barrier to dissociation by managing the enthalpic and entropic activation components. Finally, we review recent studies of the biotin dissociation pathway that address the fundamental question of how ligands exit protein binding pockets.

Full Text

Duke Authors

Cited Authors

  • Stayton, PS; Freitag, S; Klumb, LA; Chilkoti, A; Chu, V; Penzotti, JE; To, R; Hyre, D; Le Trong, I; Lybrand, TP; Stenkamp, RE

Published Date

  • December 1999

Published In

Volume / Issue

  • 16 / 1-4

Start / End Page

  • 39 - 44

PubMed ID

  • 10796983

Pubmed Central ID

  • 10796983

International Standard Serial Number (ISSN)

  • 1389-0344

Digital Object Identifier (DOI)

  • 10.1016/s1050-3862(99)00042-x

Language

  • eng