Empty spaces, how do they make a protein unstable?

ScienceDaily | 10/15/2019 | Staff
j.moomin (Posted by) Level 3
Because these excited states exist only briefly and are lowly populated they are "invisible" to most experimental methods. However, recent developments in NMR spectroscopy allow for their detection and structural investigation at atomic resolution.

In this study, the researchers used a classic model system for protein folding, the L99A mutant of T4 lysozyme. This protein has a cavity in its hydrophobic core that is large enough to fit a benzene ring (a chemical compound consisting of a ring of 6 carbon atoms).

Mulder - Team - Nuclear - Resonance - NMR

Mulder and his team used Nuclear Magnetic Resonance (NMR) spectroscopy coupled with hydrostatic pressure to monitor "invisible" excited states. High pressure favors compact states, and the protein unfolds...
(Excerpt) Read more at: ScienceDaily
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