New Insight into Solution Structure and Dynamics of Proteins, Nucleic Acids, and Viruses from Raman Optical Activity

2002 ◽  
pp. 34-49
Author(s):  
L. D. Barron ◽  
E. W. Blanch ◽  
A. F. Bell ◽  
C. D. Syme ◽  
L. Hecht ◽  
...  
Keyword(s):  
Nucleic Acids ◽  
Optical Activity ◽  
Solution Structure ◽  
Structure And Dynamics ◽  
Raman Optical Activity ◽  
Insight Into

Recent Developments in Raman Optical Activity of Biopolymers

1996 ◽  
Vol 50 (5) ◽  
pp. 619-629 ◽  
Author(s):  
L. D. Barron ◽  
L. Hecht ◽  
A. F. Bell ◽  
G. Wilson
Keyword(s):  
Secondary Structure ◽  
Nucleic Acids ◽  
Optical Activity ◽  
Solution Structure ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Raman Optical Activity ◽  
Recent Developments ◽  
Different Temperatures ◽  
Carbohydrate Components

Recent advances in Raman optical activity (ROA) instrumentation are outlined which have enhanced significantly the quality of vibrational ROA spectra of biopolymers in aqueous solution. Peptides, proteins, carbohydrates, glycoproteins, and nucleic acids now provide excellent ROA spectra which contain detailed information about solution structure. ROA spectra can be measured just as easily in D2O as in H2O solution, and, as illustrated for bovine serum albumin and concanavalin A, a comparison of the two can be highly informative. In addition to signatures of extended secondary structure, protein ROA spectra also contain signatures related to loops and turns which are valuable for studying tertiary structure and dynamics, exemplified here by a comparison of the ROA spectra of reduced lysozyme and unordered poly-L-lysine, by the ROA spectra of acid molten globule α-lactalbumin at different temperatures, which reveal a native-like tertiary fold, and by changes in the ROA spectrum of native lysozyme on binding to a saccharide inhibitor. Carbohydrate ROA spectra contain signatures of all the central features of their stereochemistry and, as shown by a comparison of laminaribiose with laminarin, can also probe extended secondary structure in polysaccharides. Results on a glycoprotein, orosomucoid, suggest that ROA can provide information about both the protein and the carbohydrate components. Preliminary results on nucleic acids are outlined with the ROA spectra of Poly(rA)·Poly(rU) and Poly(rI)·Poly(rC) shown as examples.

scholarly journals Localized molecular orbitals for calculation and analysis of vibrational Raman optical activity

2018 ◽  
Vol 20 (45) ◽  
pp. 28751-28758 ◽  
Author(s):  
Sandra Luber
Keyword(s):  
Optical Activity ◽  
Molecular Orbitals ◽  
Localized Molecular Orbitals ◽  
Raman Optical Activity ◽  
Chiral Systems ◽  
Spectroscopic Signatures ◽  
Insight Into ◽  
The Way

First calculations of vibrational Raman optical activity based on localized molecular orbitals are presented, which pave the way for novel insight into spectroscopic signatures of chiral systems.

scholarly journals Structure and Behaviour of Proteins, Nucleic Acids and Viruses from Vibrational Raman Optical Activity

2003 ◽  
Vol 17 (2-3) ◽  
pp. 101-126 ◽  
Author(s):  
Laurence D. Barron ◽  
Ewan W. Blanch ◽  
Iain H. McColl ◽  
Christoper D. Syme ◽  
Lutz Hecht ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Optical Activity ◽  
Tertiary Structure ◽  
Incident Light ◽  
Mutual Orientation ◽  
Coat Proteins ◽  
Raman Optical Activity ◽  
Sugar Ring ◽  
Polypeptide Backbone

On account of its sensitivity to chirality Raman optical activity (ROA), which may be measured as a small difference in vibrational Raman scattering from chiral molecules in right- and left-circularly polarized incident light, is a powerful probe of structure and behaviour of biomolecules in aqueous solution. Protein ROA spectra provide information on the secondary and tertiary structure of the polypeptide backbone, hydration, side chain conformation and structural elements present in denatured states. Nucleic acid ROA spectra provide information on the sugar ring conformation, the base stacking arrangement and the mutual orientation of the sugar and base rings around the C–N glycosidic link. The ROA spectra of intact viruses provide information on the folds of the coat proteins and the nucleic acid structure. The large number of structure-sensitive bands in protein ROA spectra is especially favourable for fold determination using pattern recognition techniques. This article gives a brief account of the ROA technique and presents the ROA spectra of a selection of proteins, nucleic acids and viruses that illustrate the applications of ROA spectroscopy in biomolecular research.

Raman optical activity instrument for studies of biopolymer structure and dynamics

1999 ◽  
Vol 30 (9) ◽  
pp. 815-825 ◽  
Author(s):  
Lutz Hecht ◽  
Laurence D.Barron ◽  
Ewan W. Blanch ◽  
Alasdair F. Bell ◽  
Loren A. Day
Keyword(s):  
Optical Activity ◽  
Structure And Dynamics ◽  
Raman Optical Activity ◽  
Biopolymer Structure

scholarly journals Solution Structure of Mannobioses Unravelled by Means of Raman Optical Activity

ChemPhysChem ◽  
2019 ◽  
Vol 20 (5) ◽  
pp. 695-705 ◽  
Author(s):  
Robert Pendrill ◽  
Shaun T. Mutter ◽  
Carl Mensch ◽  
Laurence D. Barron ◽  
Ewan W. Blanch ◽  
...  
Keyword(s):  
Optical Activity ◽  
Solution Structure ◽  
Raman Optical Activity
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