The relationship of bound water to the IR amide I bandwidth of albumin

Jakobsen, R. J.; Wasacz, F. M.; Brasch, J. W.; Smith, Keith B.

doi:10.1002/bip.360250409

Cited by 40 publications

(28 citation statements)

References 9 publications

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“…One might conclude from the spectral data in Figures 4 and 5 that the effect of bound water was to broaden peak areas of various conformations due to the broader distribution of energies of hydrogen bonding with water when compared to intramolecular bonding in the solid between carbonyl oxygens and amide hydrogens. This agrees with the results of Jakobsen et al (1986) on experiments with albumin.…”

Section: Resultssupporting

confidence: 93%

Effects of Bound Water on FTIR Spectra of Glycinin

Abbott

Nabetani

Sessa

et al. 1996

J. Agric. Food Chem.

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Soy protein is a major food component, but the secondary structure of its major proteins is not well established, especially after heat treatment in the presence of moisture. To study secondary structure changes that take place in glycinin upon hydration using infrared spectroscopy, the effect of bound water must be removed from the protein spectra. This study examined the effects of added water on glycinin infrared spectra. Samples hydrated from 2.6 to 95% water, but not heated, showed significant broadening in the amide I region and changes in the amide I to amide II maximum absorbance ratio as water content increased. A spectral ratio method to derive coefficients for multiplying and subtracting spectra was used to obtain the bound water component spectrum and protein component spectra. The spectrum of dry glycinin could then be regenerated by subtracting the bound water component from glycinin that had added water. Curve-fitting of deconvoluted spectra gave the same secondary structure at all levels of added water after bound water had been subtracted from the spectra (30% , 24% helical, 35% turns, and 11% unordered). Spectra of glycinin in aqueous buffer were also determined. Side-chain contributions were removed, and the resulting secondary structure was found to be 33% , 25% helical, 31% turns, and 12% unordered. This compares to 32% , 21% helical, 34% turns, and 14% unordered before side-chain contributions were subtracted. The data indicate that glycinin has the same structure in solution and in hydrated solids.

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Section: Resultssupporting

confidence: 93%

Effects of Bound Water on FTIR Spectra of Glycinin

Abbott

Nabetani

Sessa

et al. 1996

J. Agric. Food Chem.

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“…The narrowing of the Amide I bandwidth is also consistent with an increase in order. Three other types of experiments support this interpretation of the relationships of the bandwidth and order of and Amide I vibration of albumin with the amount of bound water present in the protein (13). Two of these involve changes in pH or changes in pressure of albumin molecules dissolved in saline.…”

Section: Effects Of the Environment On The Structure Of Adsorbed Protmentioning

confidence: 65%

“…After albumin as adsorbed onto a germanium ATR crystal (from a saline solution), the adsorbed film was then exposed to pure saline followed by either methanol or ethylene glycol (13,14). After subtraction of the solvent, the spectrum of the adsorbed albumin film exposed to saline was compared to the spectrum of the adsorbed albumin film exposed to either of the non-aqueous solvents.…”

Section: Effects Of the Environment On The Structure Of Adsorbed Protmentioning

confidence: 99%

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Effects of the Environment on the Structure of Adsorbed Proteins: Fourier Transform Infrared Spectroscopic Studies

Jakobsen¹,

Wasacz²

1987

ACS Symposium Series

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The protein backbone vibrations have been assigned for a group of proteins in aqueous solution using deconvoluted spectra for the assignments. These assignments were related to the secondary structure of the proteins and show the effect of one secondary structure on another. Changes in the environment of dissolved and adsorbed proteins have been followed by infrared spectroscopy and these spectral changes have been used to verify the vibrational assignments and determine the secondary structures. Very few of the infrared studies of proteins have been carried out on aqueous solutions of the proteins. Except for the work ofKoenig and Tabb (1), the few aqueous IR studies have been on single proteins. Correspondingly, most of the assignments of the backbone vibrations (the so-called Amide I, II, III, etc. vibrations) have been based on either Raman spectra of aqueous solutions (2) or on infrared spectra of proteins in the solid state (3). Where infrared solution spectra have been obtained, it has mostly been on D2O solutions (4) -not H2O solutions. Since these Amide I, II, III, etc. vibrations involve motion of the protein backbone, they are sensitive to the secondary structure of the protein and thus valid assignments are necessary in order to use infrared spectroscopy for determining the conformations of proteins.The Raman frequencies of the protein backbone vibrations are often different than the infrared frequencies and thus infrared assignments are needed for structure determinations from infrared spectra.Such structural information is needed from the 'Current address: Mattson Instruments, Inc., 1001 Fourier Court, Madison, WI 53717

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“…The main difference between these spectra is that the amide I band is a little broader when IgG is adsorbed on the hydrophobic ϩ copolymer surface. It is known that the widths of the IR amide bands depend strongly on the interaction of the polypeptide with its environment (31,32). On the other hand, the position of the amide I band is almost independent of the copolymer presence, suggesting that the secondary structures of the adsorbed protein on hydrophilic and on hydrophobic ϩ copolymer surfaces are rather similar.…”

Section: Table 2 Comparison Of the Peak Positions Obtained With The Smentioning

confidence: 94%