Raman spectroscopy of proteins

Thomas, G. J. Jr. (1999). Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct. 28, 1-27. 

Raman spectroscopy of proteins runs parallel to IR spectroscopy. The same vibrational transitions associated with the same normal vibrational modes centred on atom motions within peptide links are observed (Table 4.3 Figure 4.10). The same is true for the Raman spectroscopy of nucleic acids as well. Arguably, Raman spectroscopy of a globular protein of interest gives an even more precise characterisation of vibrational transitions than IR spectroscopy, allowing for the clear discrimination and identification of random coil structure as well as a-helix, parallel jd-sheet and antiparallel jd-sheet secondary structures. 

BG Frushour, JL Koenig. Raman Spectroscopy of proteins. In RSH Clark, RE Hester, eds. Advances in Infrared and Raman Spectroscopy Vol. I. London Hey den, 1975, pp 35-97. 

Asher S A, Chi Z, Holtz J S W, Lednev I K, Karnoup A S and Sparrow M C 1998 UV resonance Raman studies of protein structure and dynamics XWf/r int. Conf on Raman Spectroscopy ed A M Heyns (New York Wley) pp 11-14... 

Resonance Raman Spectroscopy of Iron—Oxo and Iron—Sulfur Clusters in Proteins... 

Selected entries from Methods in Enzymology [vol, page(s)] Biomolecular vibrational spectroscopy, 246, 377 Raman spectroscopy of DNA and proteins, 246, 389 resonance Raman spectroscopy of metalloproteins, 246, 416 structure and dynamics of transient species using time-resolved resonance Raman spectroscopy, 246, 460 infrared spectroscopy applied to biochemical and biological problems, 246, 501 resonance Raman spectroscopy of quinoproteins, 258, 132. 

CONTENTS Introduction to the Series An Editor s Foreword, Albert Padwa. Preface, C. Allen Bush. Raman Spectroscopy of Nucleic Acids and Their Complexes. George J. Thomas, Jr. and Masamichi Tsuboi. Oligosaccharide Conformation in Pro-tein/Carbohydrate Complexes, Anne Imberty, Yves Bourne, Christian Cambillau and Serge Perez. Geometric Requirements of Proton Transfers, Steve Scheiner. Structural Dynamics of Calcium-Binding Proteins, Robert F. Steiner. Determination of the Chemical Structure of Complex Polysaccharides, C. Abeygunawardana and C. Allen Bush. Index. 

Fig. 18.2. Raman spectroscopy of live, fixed and dried cells. Raman spectrum of a single cell construct provides a unique biochemical fingerprint , which provides a snap shot of the entire biomolecular components. The mean Raman spectra (4 separate measurements) of a single live, fixed and desiccated epithelial cell are compared (a). Fixation and desiccation influence cellular biochemistry. Desiccation distorts Raman bands describing all cellular biopolymers, especially proteins. Distinct biochemical changes in the secondary structure of proteins in the fixed cell can also be detected. Similar results were obtained in several other cells when analysed under similar conditions. Light microscope pictures of the cells in live cell culture (b), and after fixation (c) and desiccation (d) are shown. Scalebar = 10 pm. [3]...

I. Harada and H. Takeuchi, Raman and ultraviolet resonance Raman spectra of proteins and related compounds, in Advances in Spectroscopy (R. A. H. Clark and R. E. Hester, eds.), Vol. 13, John Wiley, New York, 1986. 

For example, see T. G. Spiro, The resonance Raman spectroscopy of metalloporphyrins and heme proteins, in Iron Porphyrins (A. B. P. Lever and H. B. Gray, eds.), Part II. Addison-Wesley, Reading, MA, 1983. 

W. H. Woodruff, R. B. Dyer, and J. R. Schoonover, Resonance Raman spectroscopy of blue copper proteins, in Biological Applications of Raman Spectroscopy (T. G. Spiro, ed.), Vol. 3. John Wiley, New York, 1988. 

Spiro TG (1975) Biological applications of resonance Raman-spectroscopy - Heme proteins. Proc R Soc Lond Ser A Math Phys Eng 345 89-105... 

Tsuboi M (1977) Raman Spectroscopy of Nucleic Acids and Proteins chapt 25. In Decius JC, Hexter RM (eds) Molecular Vibrations in Crystals. McGraw-Hill, New York, p 405 Tsuboi M, Shuto K, Higushi S (1968) Bull Chem Soc Japan 41 1821 Turner JJ, Pimentel GC (1963) Science 140 974... 

Stewart, S. and Fredericks, P.M. (1999) Surface-enhanced Raman spectroscopy of peptides and proteins adsorbed on an electrochemically prepared silver surface. Spectrochimica Acta A, 55, 1615-1640. 

Chumanov, G.D., Efremov, R.G., and Nabiev, LR. (1990) Surface-enhanced Raman spectroscopy of biomolecules 1. Water-soluble proteins, dipeptides and amino acids. Journal of Raman Spectroscopy, 21, 43-48. 

Vibrational spectroscopy of the electronically excited state pulse radiolysis/time-resolved resonance Raman study of the triplet y3-carotene. J Am Chem Soc 101 1355-1357 De Paula JC, Ghanotakis DF, Bowlby NR, Dekker JP, Yocum CF and Babcock GT (1990) Chlorophyll-protein interactions in Photosystem II. Resonance Raman spectroscopy of the D1 D2-cytochrome b559 complex and the 47 kDa protein. In Baltscheffsky M (ed) Current Research in Photosynthesis, pp 643-646, Kluwer Academic Publishers, Dordrecht Frank HA and Cogdell RJ (1993) Photochemistry and functions of carotenoids in Photosynthesis. In Young A and Britton G (eds) Carotenoids in Photosynthesis, pp 252-326. Chapman Hall, London... 

Pascal AA, Caron L, Rousseau B, Lapouge K, Duval JC and Robert B (1998) Resonance Raman spectroscopy of a lightharvesting protein from the brown Alga Laminaria sacchaiina. Biochemistry 37 2450-2457... 

Resonance Raman Spectroscopy and Carotenoid Stereochemistry Resonance Raman Spectroscopy of Excited States of Carotenoids Resonance Raman of Carotenoid Molecules In Vivo Light-Hanresting Proteins... 

Previous infrared studies indicate that proteins with a large amount of 3-sheet structure absorb near 1240 cm and those with a-helix stucture absorb near 1280 cm l (22,32). Absorbances for denatured albumin, reportedly containing random and 3-sheet conformations, are found at 1240 and 1260 cvT (22). These assignments correlate with the more studied Raman spectroscopy of the amide III region which has vibrations at 1230-1250 cm l for 3-sheet structure, at 1260-1290 cm for a-helix structure, and at 1240-1265 cm l for unstructured polypeptide (34,35). 

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