![]() Secondary structure and interactions of the packaged dsDNA genome of bacteriophage P22 investigated by Raman difference spectroscopy. Raman spectroscopy of filamentous bacteriophage Ff (fd, M13, f1) incorporating specifically-deuterated alanine and tryptophan side chains: Assignments and structural interpretation. UV resonance Raman spectroscopy using a new CW laser source: Convenience and experimental simplicity. Secondary structure elements typically spontaneously form as an intermediate before the. 1 The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Biochemistry 40:2522-2529.Īsher, S.A., Bormett, R.W., Chen, X.G., Lemmon, D.H., Cho, N., Peterson, P., Arrigoni, M., Spinelli, L., and Cannon, J. Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. Tyrosine Raman signatures of the filamentous virus Ff are diagnostic of non-hydrogen-bonded phenoxyls: Demonstration by Raman and infrared spectroscopy of p-cresol vapor. Conventional Raman, UV-resonance Raman, and polarized Raman techniques are surveyed.Īllemann, R.K. Here, the strengths of Raman spectroscopy are illustrated by considering recent applications that address (1) subunit folding and recognition in assembly of the icosahedral capsid of bacteriophage P22, (2) orientations of subunit main chains and side chains in native filamentous viruses, (3) roles of cysteine hydrogen bonding in the folding, assembly, and function of virus structural proteins, and (4) structural determinants of protein/DNA recognition in gene regulatory complexes. Proteins may be structural, regulatory, contractile, or protective they may serve in transport, storage, or membranes or they may be toxins or enzymes. Amino acids linked by peptide bonds form dipeptides, tripeptides or polypeptides. The OH- on a carbon atom links with the H- on a nitrogen atom to form a water molecule which is given off as each peptide bond is formed. In favorable cases, the Raman spectrum serves as an empirical signature of protein three-dimensional structure, intramolecular dynamics, and intermolecular interactions. Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. peptide bond A covalent bond formed between amino acids during protein synthesis. The spectral positions, intensities, and polarizations of the Raman bands are sensitive to protein secondary, tertiary, and quaternary structures and to side -chain orientations and local environments. The most simple and elegant arrangement is a right-handed spiral conformation known as the alpha-helix. A protein Raman spectrum comprises discrete bands representing vibrational modes of the peptide backbone and its side chains. Pauling and Corey twisted models of polypeptides to find ways of getting the backbone into regular conformations which would agree with alpha-keratin fibre diffraction data. ![]()
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