[Study of Ca2+-binding centers of parvalbumin by the distant fine structure of x-ray absorption spectra].
An investigation of Ca2+-binding centers of parvalbumin II and III by analysing distant fine structure of X-ray absorption spectra of metal was performed. Protein preparations of parvalbumin II and III in which Ca2+ was isomorphically replaced by Tb3+ were studied. For spectra analyses a standard method of Fourier transformation was used. The middle of the first absorption maximum was taken as origin for energy calculations. Comparison of spectra and modules of Fourier transformations for normalized oscillations of the X-ray spectra of absorption of the II and III components, revealed that the spectra and Fourier-transformants coincide in the 2--6 A interval. This allows to infer the coincidence of the coordinate numbers, average interatomic distances and their dispersions in Ca2+-binding centers of the two protein components.
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D005399:Fishes; D005583:Fourier Analysis; D009124:Muscle Proteins / Q000378:metabolism*; D010320:Parvalbumins / Q000378:metabolism*; D013052:Spectrometry, X-Ray Emission
D009124:Muscle Proteins; D010320:Parvalbumins; D002118:Calcium
Issledovanie Ca2+-sviazyvaiushchikh tsentrov parval'bumina po dal'neĭ tonkoĭ strukture rentgenovskikh spektrov pogloshcheniia.