Investigation of polypeptide conformational transitions with two-dimensional Raman optical activity correlation analysis, applying autocorrelation and moving window approaches

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Investigation of polypeptide conformational transitions with two-dimensional Raman optical activity correlation analysis, applying autocorrelation and moving window approaches. / Ashton, Lorna; Blanch, Ewan W.
In: Applied Spectroscopy, Vol. 62, No. 5, 05.2008, p. 469-475.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{d461d8b562614cd6adeb75583488105b,

title = "Investigation of polypeptide conformational transitions with two-dimensional Raman optical activity correlation analysis, applying autocorrelation and moving window approaches",

abstract = "The study of conformational transitions in polypeptides is not only important for the understanding of folding mechanisms responsible for the self-assembly of proteins but also for the investigation of the misfolding of proteins that can result in diseases including cystic fibrosis, Alzheimer's, and Parkinson's diseases. Our recent studies developing two-dimensional Raman optical activity (ROA) correlation analysis have proven to be successful in the investigation of polypeptide conformational transitions. However, the complexity of the ROA spectra, and the 2D correlation synchronous and asynchronous plots, makes data analysis detailed and complex, requiring great care in interpretation of 2D correlation rules. By utilizing the 2D correlation approaches of autocorrelation and moving windows it has been possible to gain further information from the ROA spectral data sets in a simpler and more consistent way. The most significant spectral intensity changes have been easily identified, facilitating appropriate interpretation of synchronous plots, and transition phases have been identified in the moving window plots, directly relating spectral intensity changes to the perturbation.",

keywords = "Raman optical activity, ROA, two-dimensional correlation, conformational transitions, poly(L-lysine), poly(L-glutamic acid), VIBRATIONAL CIRCULAR-DICHROISM, BETA-SHEET TRANSITION, UV RESONANCE RAMAN, L-GLUTAMIC ACID, POLY-L-LYSINE, ALPHA-HELIX, SECONDARY STRUCTURE, AMYLOID FIBRILS, POLY(L-GLUTAMIC ACID), PROTEIN",

author = "Lorna Ashton and Blanch, {Ewan W.}",

year = "2008",

month = may,

language = "English",

volume = "62",

pages = "469--475",

journal = "Applied Spectroscopy",

issn = "0003-7028",

publisher = "Society for Applied Spectroscopy",

number = "5",

}

RIS

TY - JOUR

T1 - Investigation of polypeptide conformational transitions with two-dimensional Raman optical activity correlation analysis, applying autocorrelation and moving window approaches

AU - Ashton, Lorna

AU - Blanch, Ewan W.

PY - 2008/5

Y1 - 2008/5

N2 - The study of conformational transitions in polypeptides is not only important for the understanding of folding mechanisms responsible for the self-assembly of proteins but also for the investigation of the misfolding of proteins that can result in diseases including cystic fibrosis, Alzheimer's, and Parkinson's diseases. Our recent studies developing two-dimensional Raman optical activity (ROA) correlation analysis have proven to be successful in the investigation of polypeptide conformational transitions. However, the complexity of the ROA spectra, and the 2D correlation synchronous and asynchronous plots, makes data analysis detailed and complex, requiring great care in interpretation of 2D correlation rules. By utilizing the 2D correlation approaches of autocorrelation and moving windows it has been possible to gain further information from the ROA spectral data sets in a simpler and more consistent way. The most significant spectral intensity changes have been easily identified, facilitating appropriate interpretation of synchronous plots, and transition phases have been identified in the moving window plots, directly relating spectral intensity changes to the perturbation.

AB - The study of conformational transitions in polypeptides is not only important for the understanding of folding mechanisms responsible for the self-assembly of proteins but also for the investigation of the misfolding of proteins that can result in diseases including cystic fibrosis, Alzheimer's, and Parkinson's diseases. Our recent studies developing two-dimensional Raman optical activity (ROA) correlation analysis have proven to be successful in the investigation of polypeptide conformational transitions. However, the complexity of the ROA spectra, and the 2D correlation synchronous and asynchronous plots, makes data analysis detailed and complex, requiring great care in interpretation of 2D correlation rules. By utilizing the 2D correlation approaches of autocorrelation and moving windows it has been possible to gain further information from the ROA spectral data sets in a simpler and more consistent way. The most significant spectral intensity changes have been easily identified, facilitating appropriate interpretation of synchronous plots, and transition phases have been identified in the moving window plots, directly relating spectral intensity changes to the perturbation.

KW - Raman optical activity

KW - ROA

KW - two-dimensional correlation

KW - conformational transitions

KW - poly(L-lysine)

KW - poly(L-glutamic acid)

KW - VIBRATIONAL CIRCULAR-DICHROISM

KW - BETA-SHEET TRANSITION

KW - UV RESONANCE RAMAN

KW - L-GLUTAMIC ACID

KW - POLY-L-LYSINE

KW - ALPHA-HELIX

KW - SECONDARY STRUCTURE

KW - AMYLOID FIBRILS

KW - POLY(L-GLUTAMIC ACID)

KW - PROTEIN

M3 - Journal article

VL - 62

SP - 469

EP - 475

JO - Applied Spectroscopy

JF - Applied Spectroscopy

SN - 0003-7028

IS - 5

ER -

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