Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron–electron resonance

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 111; no. 13; pp. E1201 - E1210
• Main Authors: Lerch, Michael T., Yang, Zhongyu, Brooks, Evan K., Hubbell, Wayne L.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 01.04.2014; National Acad Sciences
• Series: PNAS Plus
• Subjects: Animals; Apoproteins - chemistry; Atmospheric pressure; Biological Sciences; Data collection; Electron Spin Resonance Spectroscopy - methods; Electrons; Freezing; Genomics; Heterogeneity; High pressure; high pressure treatment; Hydrogen-Ion Concentration; Hydrostatic Pressure; Models, Molecular; mutants; myoglobin; Myoglobin - chemistry; Myoglobins; PNAS Plus; Protein Structure, Secondary; Proteins; Resonance; spectral analysis; Sperm Whale; Spin Labels; temperature; compressibility; dipolar spectroscopy; EPR

The dominance of a single native state for most proteins under ambient conditions belies the functional importance of higher-energy conformational states (excited states), which often are too sparsely populated to allow spectroscopic investigation. Application of high hydrostatic pressure increases...