Keywords: Amide Bands, Collagen, Proline Puckering, Raman Crystallography, Peptide, Pyrrolidine Derivative, Accuracy, Article, Complex Formation, Crystal Structure, Crystallization, Microscopy, Priority Journal, Protein Conformation, Protein Structure, Structure Analysis, Theoretical Model, Validity, X Ray Crystallography, X-Ray, Confocal, Molecular, Spectrum Analysis,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, Complesso Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, I-80134 Naples, Italy
Consorzio Bioteknet, University of Naples, Italy
Dipartimento delle Scienze Biologiche, CNISM, Università degli Studi di Napoli Federico II, Via Mezzocannone 16, I-80134 Naples, Italy
CEINGE, Biotecnologie Avanzate, Scarl, Naples, Italy
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Li, M. H., Fan, P., Brodsky, B., Baum, J., Two-dimensional NMR assignments and conformation of (Pro-Hyp-Gly) 10 and a designed collagen triple-helical peptide (1993) Biochemistry, 32, pp. 7377-7387
Carey, P. R., Dong, J., Following ligand binding and ligand reactions in proteins via Raman crystallography (2004) Biochemistry, 43, pp. 8885-8893
Thomas, G. J. J., Raman spectroscopy of protein and nucleic acid assemblies (1999) Annu. Rev. Biophys. Biomol. Struct., 28, pp. 1-27
Mikhonin, A. V., Myshakina, N. S., Bykov, S. V., Asher, S. A., UV Resonance Raman determination of polyproline II, extended 2. 51-helix, and -sheet angle energy landscape in poly-l-lysine and poly-l-glutamic acid (2005) J. Am. Chem. Soc., 127, pp. 7712-7720
Asher, S. A., Mikhonin, A. V., Bykov, S. V., UV Raman demonstrates that -helix polyalanine peptides melt to polyproline II conformations (2004) J. Am. Chem. Soc., 126, pp. 8433-8440
Garcia-Ru z, J., Gonzalez-Ramirez, L., Gavira, J., Ot lora, F., Granada Crystallisation Box: a new device for protein crystallisation by counter-diffusion techniques. (2002) Acta Cryst. D: Biol. Cryst., 58, pp. 1638-1642
Asher, S. A., Ianoul, A., Mix, G., Boyden, M. N., Karnoup, A., Diem, M., Schweitzer-Stenner, R., Dihedral angle dependence of the amide III vibration: a uniquely sensitive UV resonance Raman secondary structural probe (2001) J. Am. Chem. Soc., 123, pp. 11775-11781
Howell, N. K., Arteaga, G., Nakai, S., Li-Chan, E. C. Y., Raman spectral analysis in the C-H stretching region of proteins and amino acids for investigation of hydrophobic interactions (1999) J. Agric. Food Chem., 47, pp. 924-933
Apetri, M. M., Maiti, N. C., Zagorski, M. G., Carey, P. R., Anderson, V. E., Secondary structure of -synuclein oligomers: characterization by Raman and Atomic Force Microscopy (2006) J. Mol. Biol., 355, pp. 63-71
Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10)
Model biopolymers are powerful tools to guide the interpretation of physical properties in complex systems. (Pro-Pro-Gly)(10), (PPG)(10), is a collagen-model peptide, whose structure is known at high resolution. Herein, Raman microscopy data of (PPG)(10) powders and single crystals are reported. The spectra interpretation leads to an accurate assignment of three well-resolved amide bands corresponding to the three peptide bonds (PP, PG and GP) present in the (PPG)(10) structure. These data together with the availability of torsional angles phi and Psi derived from the high-resolution crystal structure, provide the opportunity to test the validity of theoretical equations for the calculation of non-canonical amide III bands and represent a reference for theoretical calculations of vibrational spectra and for polyproline II detection in complex proteins. Spectroscopic data do not support the indication of two distinct and equally populated up and down conformations of the pyrrolidine rings observed in the (PPG)(10) crystal structure. (c) 2008 Elsevier B.V. All rights reserved.
Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10)