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