Aggregation of chymotrypsinogen : portrait by infrared spectroscopy

DOIResolve DOI: http://doi.org/10.1016/0167-4838(92)90353-F
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Volume1121
Issue1-2
Pages183188; # of pages: 6
SubjectHigh pressure; Temperature; Protein; Aggregation; Secondary structure; Infrared spectroscopy; Denaturation
AbstractChanges in the secondary structure and aggregation of chymotrypsinogen were investigated by infrared difference spectroscopy in conjunction with temperature and pressure tuning IR spectroscopy; both the amide I′ band and side chain bands were studied. A prominent component of the amide I′ band in the difference spectrum obtained upon cooling a chymotrypsinogen solution, or increasing the hydrostatic pressure, was observed in the region between 1627 and 1622 cm⁻¹. Under denaturing conditions a white gel was formed, which is attributed to irreversible self-association or aggregation. This process was accompanied by the appearance of two new amide I′ bands in the infrared spectrum of the protein: a very strong band at 1618 cm⁻¹ and a weak band at 1685 cm⁻¹. These bands are assigned to peptide segments with anti-parallel aligned β-strands.
Publication date
LanguageEnglish
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada; NRC Steacie Institute for Molecular Sciences
Peer reviewedYes
NRC number40
NPARC number9148508
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Record identifier888a703f-dbe0-42dd-b731-62d22baa4690
Record created2009-06-25
Record modified2016-12-22
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