Abstract
Combination of hetero-nuclear two-dimensional NMR spectroscopy with pressure in the range 1~4 kbar enables one to detect and analyze structures of higher energy conformers of proteins existing between the fully folded and the fully unfolded. The idea is based on the recognition that partial molar volume of a protein decreases in parallel with the loss of its conformational order. Available information suggests that the structure determined at high pressure is generally related to the structure at 1 bar by linear compression. The method opens a new area of structural biology that will lead to better understanding of protein function, folding and conformational disease.
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Akasaka, K. (2003). High Pressure NMR Spectroscopy Characterizes Higher Energy Conformers of Proteins. In: Winter, R. (eds) Advances in High Pressure Bioscience and Biotechnology II. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-05613-4_2
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DOI: https://doi.org/10.1007/978-3-662-05613-4_2
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