Article
Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues.
Biochemistry - 11 Jul 1995
Svensson M, Jonasson P, Freskgård P O, Jonsson B H, Lindgren M, Mårtensson L G, Gentile M, Borén K, Carlsson U
Abstract excerpt
Several conformation-sensitive parameters have shown that human carbonic anhydrase II exists as a stable and compact equilibrium folding intermediate of molten globule type. In this study we have continued a previously initiated mapping of the intermediate structure. Cys residues were engineered, one at a time, into various regions of the protein structure, so as to obtain chemically reactive probes and handles...
Topics
- Carbonic Anhydrases
- Cysteine
- Electron Spin Resonance Spectroscopy
- Enzyme Stability
- Fluorescent Dyes
- Humans
- Molecular Probes
- Molecular Structure
- Mutation
- Protein Conformation