[Secondary structure of tubulin on the data of Fourier transform infrared spectroscopy ].
Fourier transform infrared technique is used for identifying secondary structure of GTP/GDP tubulin in the absorbency region of its amide-I band. With this technique the band was initially resolved for 3 main and 4 satellite maxima, subsequently taken as starting values for computer resolution of the band into components of Gaussian line shape. A resolution of the spectrum into components was carried out with the FUMILI software; the resolution error was 1.5%. Improved maxima positions for the resolved components of GTP tubulin spectrum are as follows: 1682.2; 1663.7; 1653.2; 1633.4; 1625.4; 1614.0; 1605.7 cm-1, each assigned to the vibrations of a definite structural type of the protein. The main part of the structure, approximately 50%, corresponds to beta-antiparallel sheet, the contribution of alpha-coils is about of 25%. GDP tubulin shows the contribution of beta-antiparallel sheet to be greater and the contribution of alpha-coil to be less than in GTP tubulin. The difference in the maxima positions of GTP and GDP tubulin spectra does not exceed the value of +/- 3 cm-1.
Tulub
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AA
St. Petersburg State University.
D000818:Animals; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013552:Swine; D014404:Tubulin / Q000737:chemistry*
D014404:Tubulin
Vtorichnaia struktura tubulina po dannym IK Fur'e-spektroskopicheskogo issledovaniia.