Light induced states in MbCO denatured with guanidine hydrochloride

被引:6
作者
Natali, F
Moretti, L
Boffi, F
Bianconi, A
Della Longa, S
Castellano, AC [1 ]
机构
[1] Univ Roma La Sapienza, Dipartimento Fis, I-00185 Rome, Italy
[2] Univ Roma La Sapienza, Ist Nazl Fis Mat, I-00185 Rome, Italy
[3] Univ Aquila, Dipartimento Med Sperimentale, I-67100 Laquila, Italy
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 1998年 / 27卷 / 01期
关键词
optical spectroscopy; protein folding; protein denaturation;
D O I
10.1007/s002490050104
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30-80 K. The changes in the Sorer band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein.
引用
收藏
页码:1 / 7
页数:7
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