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Title: FTIR 2D correlation spectroscopy of α(1) and α(2) fractions of an alkali-pretreated gelatin
Authors: Chys, Pieter
Gielens, Constant
Meersman, Filip # ×
Issue Date: Feb-2011
Publisher: Elsevier/North Holland
Series Title: Biochimica et Biophysica Acta vol:1814 issue:2 pages:318-25
Abstract: An alkali-pretreated gelatin (pI~4.9) was fractionated by means of alcohol coacervation and semi-preparative gel chromatography. The thermal responses of the isolated α fractions, the coacervate and the total gelatin were investigated by 2D-correlation FTIR spectroscopy in the amide I band region (1600-1700cm(-1)). The gelation temperature was the same for all examined samples (24.5°C) while the melting temperature of the α(2) fraction was lower (30°C) than that of the other samples (32.5°C). The 2D COS plots indicate that on cooling (gelation) the core sequence of conformational changes is the same for all samples. On heating, however, the α(2) fraction deviates from the α(1)-containing samples and shows an earlier disappearance of the triple helix signal in the event sequence. The lower melting temperature (less thermostable gelatin gel) of the α(2) fraction thus results from a different conformational cascade of the α(2) chains upon melting. In all samples the initial conformational changes take place in the β-turns, providing further evidence for the models proposed previously.
URI: 
ISSN: 0006-3002
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Imaging and Photonics
Chemistry - miscellaneous
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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