2010
DOI: 10.1016/j.ijbiomac.2010.06.001
|View full text |Cite
|
Sign up to set email alerts
|

Dissecting the key residues crucial for the species-specific thermostability of muscle-type creatine kinase

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
2
0

Year Published

2012
2012
2022
2022

Publication Types

Select...
4

Relationship

1
3

Authors

Journals

citations
Cited by 4 publications
(2 citation statements)
references
References 49 publications
0
2
0
Order By: Relevance
“…Therefore, it has been suggested previously that the enzyme active site is usually situated in a limited region of the enzyme molecule that is more flexible than the enzyme molecule as a whole [17]. Recently, alterations of domain interactions by mutations of CK were applied as the model of studying multimeric (multidomain) protein folding and revealed that interactions between intra-and inter-subunit domain modified the kinetic refolding manner [18,19].…”
Section: Introductionmentioning
confidence: 99%
“…Therefore, it has been suggested previously that the enzyme active site is usually situated in a limited region of the enzyme molecule that is more flexible than the enzyme molecule as a whole [17]. Recently, alterations of domain interactions by mutations of CK were applied as the model of studying multimeric (multidomain) protein folding and revealed that interactions between intra-and inter-subunit domain modified the kinetic refolding manner [18,19].…”
Section: Introductionmentioning
confidence: 99%
“…Through chemical and/or thermal denaturation, the mechanisms of inactivation and multistate folding of CK have been investigated extensively, using numerous biophysical methods including ultraviolet absorption, fluorescence, infrared spectrum, circular dichroism and sedimentation velocity 3 4 5 6 . In addition, the presence of several isoforms of CK in various tissues and/or subcellular organelles enables the study of molecular evolution and environmental adaptation using this enzyme 7 8 .…”
mentioning
confidence: 99%