FEBS Letters | |
Protein dynamics An overview on flash‐photolysis over broad temperature ranges | |
Di Iorio, Ernesto E.1  | |
[1] Laboratorium für Biochemie I, Eidgenössische Technische Hochshule, Universitätsstrasse 16, 8092 Zurich, Switzerland | |
关键词: Protein-dynamics; Heme-protein; Kinetics; Flash-photolysis; Protein-relaxation; Low-temperature; | |
DOI : 10.1016/0014-5793(92)80893-L | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Ligand binding kinetics to heme-proteins between 40 and 300 K point to a regulatory role of protein dynamics. A protein-specific susceptibility of the heme-iron reactivity to dynamic fluctuations emerges from the distribution of reaction enthalpies derived from flash-photolysis measurements below ca. 180 K; we quantify it in terms of ‘intramolecular viscosity’, postulating that narrow low-temperature enthalpy distributions correspond to low internal viscosity and vice versa. The thermal evolution of ligand binding kinetics suggests, with other results, an interplay between high-frequency transitions of the amino acid side chains and low-frequency collective motions as a possible regulatory mechanism of protein dynamics.
【 授权许可】
Unknown
【 预 览 】
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