LOCAL AND GLOBAL DYNAMICS DURING THE FOLDING OF ESCHERICHIA-COLI DIHYDROFOLATE-REDUCTASE BY TIME-RESOLVED FLUORESCENCE SPECTROSCOPY
LOCAL AND GLOBAL DYNAMICS DURING THE FOLDING OF ESCHERICHIA-COLI DIHYDROFOLATE-REDUCTASE BY TIME-RESOLVED FLUORESCENCE SPECTROSCOPY
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DOI:
10.1021/bi00006a007
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发表时间:
1995-02-14
期刊:
影响因子:
2.9
通讯作者:
MATTHEWS, CR
中科院分区:
文献类型:
--
作者:
JONES, BE;BEECHEM, JM;MATTHEWS, CR
Time-resolved fluorescence techniques were utilized to monitor the kinetic refolding reaction of Escherichia call dihydrofolate reductase (DHFR). Measurements of emission and anisotropy decay lifetimes of both the five intrinsic tryptophan residues and the fluorescent probe 1 anilinonaphthalene-8-sulfonate (ANS) during the folding reaction were used to characterize the compactness and development of tertiary structure in transient intermediates formed during the folding of DHFR. Experiments monitoring bound ANS show that a rapidly-formed intermediate (