Time-resolved FTIR difference spectroscopy as tool for investigating refolding reactions of ribonuclease T1 synchronized with trans -> cis prolyl isomerization

Item Type:	Article
Title:	Time-resolved FTIR difference spectroscopy as tool for investigating refolding reactions of ribonuclease T1 synchronized with trans -> cis prolyl isomerization
Creators Name:	Moritz, R. and Reinstadler, D. and Fabian, H. and Naumann, D.
Abstract:	The structurally well-characterized enzyme ribonuclease T1 was used as a model protein to further evaluate time-resolved Fourier transform IR difference spectroscopy in conjunction with temperature-jump techniques as a useful detection technique for protein folding studies. Compared to the wild-type protein, it was confirmed that the lack of one cis-proline bond at position 55 of the S54G/P55N variant is sufficient to significantly simplify and accelerate the refolding process. This result was sustained by the characterization of the early refolding events that occurred within the experimental dead time.
Keywords:	Folding Kinetics, Prolyl Peptide Bond Isomerization, Protein Folding, S54G/P55N Ribonuclease T1, Temperature Jump, Time-Resolved Fourier Transform IR Spectroscopy
Source:	Biopolymers
ISSN:	0006-3525
Publisher:	Wiley
Volume:	67
Number:	3
Page Range:	145-155
Date:	18 April 2002
Official Publication:	https://doi.org/10.1002/bip.10083
PubMed:	View item in PubMed

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