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pH-induced conformational transitions in alpha-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows

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pH-induced conformational transitions in alpha-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows. / Ashton, Lorna; Blanch, Ewan W.
In: Journal of Molecular Structure, Vol. 974, No. 1-3, 16.06.2010, p. 132-138.

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Ashton L, Blanch EW. pH-induced conformational transitions in alpha-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows. Journal of Molecular Structure. 2010 Jun 16;974(1-3):132-138. doi: 10.1016/j.molstruc.2010.03.005

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@article{7b29955d78ed49f09ae52748a457ec9a,
title = "pH-induced conformational transitions in alpha-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows",
abstract = "Raman spectroscopy is being increasingly applied to the investigation of conformational transitions in polypeptides and proteins, and in particular protein unfolding, due to its ability to monitor changes in secondary structure. Here we focus on the application of two different two-dimensional correlation methods, autocorrelation and moving windows techniques, to investigate the pH-induced conformational transitions in alpha-lactalbumin monitored with Raman scattering. From our results we have identified three distinct stages in the conformational transition occurring at ranges similar to pH 6.5-4.6, similar to pH 4.6-3.6 and similar to pH 3.6-1.8, suggesting the existence of three possible conformational species. The first two transition phases the conformational changes are predominantly occurring in the backbone secondary structure, while in the final transition phase changes are occurring in both secondary structure and side chain residue solvent exposure. (C) 2010 Elsevier B.V. All rights reserved.",
keywords = "2D correlation, Raman, Moving windows, Protein, alpha-Lactalbumin, MOLTEN GLOBULE STATE, UV RESONANCE RAMAN, INFRARED CORRELATION SPECTROSCOPY, OPTICAL-ACTIVITY, STRUCTURAL-CHARACTERIZATION, SECONDARY STRUCTURE, POLY(L-GLUTAMIC ACID), CORRELATION SPECTRA, BETA-LACTOGLOBULIN, PHASE-TRANSITIONS",
author = "Lorna Ashton and Blanch, {Ewan W.}",
year = "2010",
month = jun,
day = "16",
doi = "10.1016/j.molstruc.2010.03.005",
language = "English",
volume = "974",
pages = "132--138",
journal = "Journal of Molecular Structure",
issn = "0022-2860",
publisher = "Elsevier",
number = "1-3",
note = "5th International Symposium on Two Dimensional Correlation Spectroscopy ; Conference date: 05-08-2009 Through 07-08-2009",

}

RIS

TY - JOUR

T1 - pH-induced conformational transitions in alpha-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows

AU - Ashton, Lorna

AU - Blanch, Ewan W.

PY - 2010/6/16

Y1 - 2010/6/16

N2 - Raman spectroscopy is being increasingly applied to the investigation of conformational transitions in polypeptides and proteins, and in particular protein unfolding, due to its ability to monitor changes in secondary structure. Here we focus on the application of two different two-dimensional correlation methods, autocorrelation and moving windows techniques, to investigate the pH-induced conformational transitions in alpha-lactalbumin monitored with Raman scattering. From our results we have identified three distinct stages in the conformational transition occurring at ranges similar to pH 6.5-4.6, similar to pH 4.6-3.6 and similar to pH 3.6-1.8, suggesting the existence of three possible conformational species. The first two transition phases the conformational changes are predominantly occurring in the backbone secondary structure, while in the final transition phase changes are occurring in both secondary structure and side chain residue solvent exposure. (C) 2010 Elsevier B.V. All rights reserved.

AB - Raman spectroscopy is being increasingly applied to the investigation of conformational transitions in polypeptides and proteins, and in particular protein unfolding, due to its ability to monitor changes in secondary structure. Here we focus on the application of two different two-dimensional correlation methods, autocorrelation and moving windows techniques, to investigate the pH-induced conformational transitions in alpha-lactalbumin monitored with Raman scattering. From our results we have identified three distinct stages in the conformational transition occurring at ranges similar to pH 6.5-4.6, similar to pH 4.6-3.6 and similar to pH 3.6-1.8, suggesting the existence of three possible conformational species. The first two transition phases the conformational changes are predominantly occurring in the backbone secondary structure, while in the final transition phase changes are occurring in both secondary structure and side chain residue solvent exposure. (C) 2010 Elsevier B.V. All rights reserved.

KW - 2D correlation

KW - Raman

KW - Moving windows

KW - Protein

KW - alpha-Lactalbumin

KW - MOLTEN GLOBULE STATE

KW - UV RESONANCE RAMAN

KW - INFRARED CORRELATION SPECTROSCOPY

KW - OPTICAL-ACTIVITY

KW - STRUCTURAL-CHARACTERIZATION

KW - SECONDARY STRUCTURE

KW - POLY(L-GLUTAMIC ACID)

KW - CORRELATION SPECTRA

KW - BETA-LACTOGLOBULIN

KW - PHASE-TRANSITIONS

U2 - 10.1016/j.molstruc.2010.03.005

DO - 10.1016/j.molstruc.2010.03.005

M3 - Journal article

VL - 974

SP - 132

EP - 138

JO - Journal of Molecular Structure

JF - Journal of Molecular Structure

SN - 0022-2860

IS - 1-3

T2 - 5th International Symposium on Two Dimensional Correlation Spectroscopy

Y2 - 5 August 2009 through 7 August 2009

ER -