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How and why internal cavities destabilize proteins
Author(s) -
Mulder Frans AA.,
Xue Mengjun,
Yoshimura Yuichi,
Kitahara Ryo
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.792.22
Subject(s) - hydrostatic pressure , van der waals force , protein stability , chemistry , physics , thermodynamics , biochemistry , organic chemistry , molecule
Proteins are marginally stable as a consequence of the large and opposing contributions from enthalpy and entropy to the folded state. The microscopic contributions to the total system ΔS and ΔH are still highly enigmatic. Here, we use hydrostatic pressure ‐– coupled to NMR spectroscopy detection – to explore the protein energy landscape in residue‐specific detail. As the conjugate of pressure is volume, this approach offers a mild and clearly defined perturbation of the system, as opposed to mutagenesis, temperature or denaturants. We could thus directly examine the Van der Waals contribution to stability. Pressure‐variation also allowed us to detect several partially unfolded states that consist of cooperative modules, a result that argues for a rather discrete route that connects the folded and unfolded forms of a protein. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .