## Abstract Protein–protein interactions were measured for ovalbumin and for lysozyme in aqueous salt solutions. Protein–protein interactions are correlated with a proposed potential of mean force equal to the free energy to desolvate the protein surface that is made inaccessible to the solvent due
Analyzing protein–protein interactions in cell membranes
✍ Scribed by Anja Nohe; Nils O. Petersen
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 287 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Interactions among membrane proteins regulate numerous cellular processes, including cell growth, cell differentiation and apoptosis. We need to understand which proteins interact, where they interact and to which extent they interact. This article describes a set of novel approaches to measure, on the surface of living cells, the number of clusters of proteins, the number of proteins per cluster, the number of clusters or membrane domains that contain pairs of interacting proteins and the fraction of one protein species that interacts with another protein within these domains. These data can then be interpreted in terms of the function of the protein‐protein interactions. BioEssays 26:196–203, 2004. © 2004 Wiley Periodicals, Inc.
📜 SIMILAR VOLUMES
Protein-protein and protein-salt interactions have been obtained for ovalbumin in solutions of ammonium sulfate and for lysozyme in solutions of ammonium sulfate, sodium chloride, potassium isothiocyanate, and potassium chloride. The two-body interactions between ovalbumin molecules in concentrated
The free energy difference between folded and unfolded state is about the same for most proteins and it is not more than the energy of a few noncovalent interactions. In addition to the numerous noncovalent interactions, some proteins contain one or more disulfide bonds, which, as covalent crosslink