Exploring the entire conformational space of proteins by high-pressure NMR
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| 024 | 7 | 0 | |a 10.1351/pac200375070927 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1351/pac200375070927 | ||
| 100 | 1 | |a Akasaka |D Kazuyuki |u Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama 649-6493, Japan and Cellular Signaling Laboratory, RIKEN Harima Institute, Hyogo 679-5148, Japan | |
| 245 | 1 | 0 | |a Exploring the entire conformational space of proteins by high-pressure NMR |h [Elektronische Daten] |c [Kazuyuki Akasaka] |
| 520 | 3 | |a A protein in solution is a thermodynamic entity, spanning, in principle, the entire allowed conformational space from the fully folded N to the fully unfolded U. Although some alternately or partially folded higher-energy conformers may coexist with N and U, they are seldom detected spectroscopically because their populations are usually quite low under physiological conditions. I describe here a new type of experiment, a combination of multidimensional NMR spectroscopy with pressure, that is capable of detecting and analyzing structures and thermodynamic stability of these higher-energy conformers. The idea is based on the finding that under physiological conditions the conformational order of a globular protein normally decreases in parallel with its partial molar volume (negative δV), so that under equilibrium conditions, the population is shifted to a less and-less-ordered conformer with increasing pressure. In principle, with the high space resolution of the multidimensional NMR, the method enables one to explore protein structure and stability in atomic detail in a wide conformational space from N to U with pressure and temperature as variables. The method will provide us with a strong basis for understanding the fundamental phenomena of proteins:function, folding, and aggregation. | |
| 540 | |a © 2013 Walter de Gruyter GmbH, Berlin/Boston | ||
| 773 | 0 | |t Pure and Applied Chemistry |d De Gruyter |g 75/7(2003-01-01), 927-936 |x 0033-4545 |q 75:7<927 |1 2003 |2 75 |o pac | |
| 856 | 4 | 0 | |u https://doi.org/10.1351/pac200375070927 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1351/pac200375070927 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 100 |E 1- |a Akasaka |D Kazuyuki |u Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama 649-6493, Japan and Cellular Signaling Laboratory, RIKEN Harima Institute, Hyogo 679-5148, Japan | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Pure and Applied Chemistry |d De Gruyter |g 75/7(2003-01-01), 927-936 |x 0033-4545 |q 75:7<927 |1 2003 |2 75 |o pac | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||