2008
DOI: 10.1016/j.saa.2007.10.035
|View full text |Cite
|
Sign up to set email alerts
|

The effect of Trp83 mutant on the properties of CopC

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

0
2
0

Year Published

2009
2009
2014
2014

Publication Types

Select...
2
1

Relationship

0
3

Authors

Journals

citations
Cited by 3 publications
(2 citation statements)
references
References 22 publications
0
2
0
Order By: Relevance
“…When the tryptophan residue 83 is mutated as leucine residue the protein is nearly immeasurable by fluorescence. Meanwhile the mutagenesis make the ability of binding to Cu(II), the thermal stability of apoCopC be decreased [28]. The important role of the tryptophan residue 83 is not only in using as a fluorescence probe but also in keeping the -sandwich hydrophobic structure.…”
Section: The Unfolding Of Copcmentioning
confidence: 99%
“…When the tryptophan residue 83 is mutated as leucine residue the protein is nearly immeasurable by fluorescence. Meanwhile the mutagenesis make the ability of binding to Cu(II), the thermal stability of apoCopC be decreased [28]. The important role of the tryptophan residue 83 is not only in using as a fluorescence probe but also in keeping the -sandwich hydrophobic structure.…”
Section: The Unfolding Of Copcmentioning
confidence: 99%
“…19 Once it unfolds, no copper(II) would be bound, or copper(II) would not affect on fluorescence emission of apo-CopC. If there are only native apo-CopC and unfolding states during the denaturation process, the capacity of copper(II) binding would be decided only by the fraction of protein keeping the native fold.…”
Section: Two-state Model In Thermodynamicsmentioning
confidence: 99%