title: [Study of calcium binding to calmodulin using laser raman spectroscopy].
abstract: Laser Raman spectroscopy has been used to study calcium binding to calmodulin, Ca2+-dependent regulator protein. Cation binding accompanied by spectral changes of tyrosine residues in the regions of Fermi-resonance doublet and 1600-1620 cm-1, of some carboxylate-containing residues, amide I, III and C-C(N) skeletal vibrations. Amide III contour analysis and calculations of Amide I contours show that complexation causes peptide backbone conformational changes characterized mainly by increased alpha-helical content.
mesh_terms: D000595:Amino Acid Sequence; D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
chemical_list: D002147:Calmodulin; D002118:Calcium
vernacular_title: Izuchenie sviazyvania kal'tsiia kal'modulinom metodom lazernoĭ spektroskopii kombinatsionnogo rasseianiia.