Structural Distributions, Fluctuations and Conformational Changes in Proteins Investigated by Mössbauer Spectroscopy and X-Ray Structure Analysis

Autor:	Fritz Parak
Rok vydání:	1989
Předmět:	chemistry.chemical_compound Materials science Structure analysis Myoglobin chemistry Chemical physics Protein dynamics Mössbauer spectroscopy Extrapolation X-ray Molecule Oxygen binding
Zdroj:	The Enzyme Catalysis Process ISBN: 9781475716092
DOI:	10.1007/978-1-4757-1607-8_14
Popis:	This contribution shows how X-ray structure analysis and Mossbauer spectroscopy can be used as complementary methods in the investigation of protein dynamics. X-ray analysis measures structural distributions via mean square displacements without having any time resolution. Mossbauer spectroscopy on 57Fe labels dynamics on a time scale faster 100 ns. Even in the extrapolation to T = 0 K myoglobin has no well defined structure with one energy minimum. The molecules are in different conformational substates. At physiological temperatures the structural distribution in the liganded (or unliganded) conformation is larger than the structural differences between these conformations. Fluctuations through conformational substates and changes of the conformation are highly correlated. The structure distribution around the heme iron influences the oxygen binding.
Databáze:	OpenAIRE
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