Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature.

Journal article

We have used low temperatures (down to -20°C) and high pressures (up to 2000 bar) to populate low-lying excited state conformers of hen lysozyme, and have analyzed their structures site-specifically using (15)N/(1)H two-dimensional HSQC NMR spectroscopy. The resonances of a number of residues were found to be selectively broadened, as the temperature was lowered at a pressure of 2000 bar. The resulting disappearance of cross-peaks includes those of residues in the β-domain of the protein and ...

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Authors: Kamatari, Y; Smith, L; Dobson, C; Akasaka, K

• Publication status: Published
• Journal: Biophysical chemistry
• Volume: 156
• Issue: 1
• Pages: 24-30
• Publication date: 2011-06-01
• DOI: 10.1016/j.bpc.2011.01.009
• EISSN: 1873-4200
• ISSN: 0301-4622
• Language: English
• Keywords: Pressure; Models, Molecular; Cold Temperature; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; Protein Conformation; Water; Animals; Chickens; Muramidase; Protein Unfolding