Premium
IR spectroscopic studies of major cellular components. III. Hydration of protein, nucleic acid, and phospholipid films
Author(s) -
Pevsner Alex,
Diem Max
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10416
Subject(s) - chemistry , nucleic acid , phospholipid , absorption (acoustics) , analytical chemistry (journal) , hydrogen bond , infrared spectroscopy , solvent , spectral line , amide , crystallography , molecule , chromatography , organic chemistry , membrane , biochemistry , optics , physics , astronomy
The IR absorption spectra of protein, DNA, RNA, and phospholipid films as a function of the water content are reported. We find that the hydration of protein films affects the peak intensity of amide I and amide II bands and the shape of the amide III band. For nucleic acids, the symmetric (ν S PO 2 − ) and antisymmetric (ν AS PO 2 − ) stretching vibrations of the phosphate linkage are the most affected by hydration, because both intensity changes and frequency shifts are observed. The spectra of phospholipid films are also sensitive to hydration, and they exhibit changes in the peak intensities and frequencies of both ν S PO 2 −and ν AS PO 2 −vibrations. We interpret the spectral differences between water saturated and dried films both in terms of structural changes and the change in the local dielectric in the vicinity of the polar and solvent exposed groups. In addition, we observe that the most significant change in the absorption intensity, frequency, and shape of the water sensitive vibrations occurs at high hydration levels. The principal component analysis of hydration results and the kinetics of water removal from sample films are also discussed. In addition, protein spectra acquired using film and KBr pellet sampling techniques are compared. © 2003 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy), 2003