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Time‐resolved FTIR difference spectroscopy as tool for investigating refolding reactions of ribonuclease T1 synchronized with trans → cis prolyl isomerization
Author(s) -
Moritz Ralf,
Reinstädler Diane,
Fabian Heinz,
Naumann Dieter
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10083
Subject(s) - chemistry , isomerization , fourier transform infrared spectroscopy , ribonuclease , folding (dsp implementation) , protein folding , cis–trans isomerism , proline , fourier transform , spectroscopy , crystallography , stereochemistry , amino acid , organic chemistry , biochemistry , catalysis , rna , chemical engineering , mathematical analysis , physics , electrical engineering , quantum mechanics , mathematics , engineering , gene
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. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 67: 145–155, 2002