High-Pressure EPR and Site-Directed Spin Labeling for Mapping Molecular Flexibility in Proteins

• Published in: Methods in enzymology Vol. 564; p. 29
• Main Authors: Lerch, Michael T, Yang, Zhongyu, Altenbach, Christian, Hubbell, Wayne L
• Format: Journal Article
• Language: English
• Published: United States 2015
• Subjects: Animals; Electron Spin Resonance Spectroscopy - instrumentation; Electron Spin Resonance Spectroscopy - methods; Equipment Design; Humans; Models, Molecular; Pressure; Protein Conformation; Protein Folding; Proteins - chemistry; Spin Labels; Thermodynamics; Double electron-electron resonance; Electron paramagnetic resonance; Protein dynamics; Conformational exchange; High pressure; Protein compressibility

High hydrostatic pressure is a powerful probe of protein conformational flexibility. Pressurization reveals regions of elevated compressibility, and thus flexibility, within individual conformational states, but also shifts conformational equilibria such that "invisible" excited states bec...