Studying the X-ray absorption fine structure spectra of a protein monolayer on liquids. The possibilities of multi-pass technique.

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For the first time, the extended fine structure of the absorption spectra for a protein monolayer on a liquid surface has been measured. We used as a test object human serum albumin treated with zinc chloride solution at a critically low concentration (3.6 × 10–7 M), which is comparable to the zinc concentration in blood serum. A multi-pass technique for detecting fluorescence radiation under total external reflection conditions was applied. The temporal stability of the Zn K-edge absorption spectra was examined using weighted regression analysis. It is shown that the error of the oscillating part of the total spectrum did not exceed 1%, which allowed to determine the radius of the first coordination sphere with an accuracy of ±0.01 Å.

作者简介

N. Novikova

National Research Center “Kurchatov Institute”

Email: nn-novikova07@yandex.ru
123182, Moscow, Russia

A. Trigub

National Research Center “Kurchatov Institute”

123182, Moscow, Russia

A. Rogachev

National Research Center “Kurchatov Institute”

123182, Moscow, Russia

G. Yalovega

Southern Federal University

Faculty of Physics, 344090, Rostov-on-Don, Russia

V. Lysenko

Southern Federal University

Faculty of Physics, 344090, Rostov-on-Don, Russia

E. Pronina

Southern Federal University

Faculty of Physics, 344090, Rostov-on-Don, Russia

O. Kosmachevskaya

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology”, Russian Academy of Sciences

119071 Russia

A. Topunov

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology”, Russian Academy of Sciences

119071 Russia

S. Yakunin

National Research Center “Kurchatov Institute”

123182, Moscow, Russia

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