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• W2085295189 endingPage "813" @default.
• W2085295189 startingPage "783" @default.
• W2085295189 abstract "The amide I band in the laser Raman spectrum of proteins has been resolved into six components, each representing residues in a different type of secondary structure. These structure types are ordered or bihydrogen-bonded helix (believed to be located in the center of helical segments), disordered or monohydrogen-bonded helix (believed to be located at the ends of helical segments), antiparallel beta sheet, parallel beta sheet, reverse turn, and undefined. The Raman spectrum representing 100% of each type of residue conformation has been computed from the solvent-subtracted Raman spectra of ten proteins with known secondary structure, plus poly-l-lysine using a least-squares solution of the overdetermined system of equations. Linear combinations of these reference spectra were then fitted to the experimental amide I spectra of these and other proteins to estimate the fractions of residues in these conformations. Statistical tests suggest that the discrimination between bihydrogen-bonded helix and monohydrogen-bonded helix is significant as is the discrimination between parallel and antiparallel β-sheet. However, the discrimination between random structure and turns has not yet been accomplished by these studies. The absolute difference between X-ray and Raman estimates of structure for 17 protein samples is generally less than 6%. We conclude that detailed and reasonably accurate estimates of secondary structure can be derived from the amide I spectra of proteins." @default.
• W2085295189 created "2016-06-24" @default.
• W2085295189 creator A5032436971 @default.
• W2085295189 creator A5042023426 @default.
• W2085295189 date "1981-11-01" @default.
• W2085295189 modified "2023-10-02" @default.
• W2085295189 title "Determination of the secondary structure of proteins from the amide I band of the laser Raman spectrum" @default.
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• W2085295189 doi "https://doi.org/10.1016/0022-2836(81)90127-3" @default.
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