ArticleBiophysical journal2005
Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Tongue sole creatine kinases function as DAMP and activate antimicrobial immunityFrontiers in immunology · 2023Article
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- A single residue substitution accounts for the significant difference in thermostability between two isoforms of human cytosolic creatine kinase.Scientific reports · 2016Article
- Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces.Extremophiles : life under extreme conditions · 2015Article
- Search by proteins for their DNA target site: 2. The effect of DNA conformation on the dynamics of multidomain proteins.Nucleic acids research · 2014Article
- Article
- Effects of the Fc-III tag on activity and stability of green fluorescent protein and human muscle creatine kinase.Protein science : a publication of the Protein Society · 2013Article
- A study of the mechanism of the chaperone-like function of an scFv of human creatine kinase by computer simulation.PloS one · 2013Article
- Biochemical and biophysical characterization of the deadenylase CrCaf1 from Chlamydomonas reinhardtii.PloS one · 2013Article
- Chaperone-like effect of the linker on the isolated C-terminal domain of rabbit muscle creatine kinase.Biophysical journal · 2012Article
- Article
- Conformational transitions of the catalytic domain of heme-regulated eukaryotic initiation factor 2α kinase, a key translational regulatory molecule.Journal of fluorescence · 2012Article
- Conformational transitions in Ariesaema curvatum lectin: characterization of an acid induced active molten globule.Journal of fluorescence · 2011Article
- Stability of domain structures in multi-domain proteins.Scientific reports · 2011Article
- Article
- The congenital cataract-linked G61C mutation destabilizes γD-crystallin and promotes non-native aggregation.PloS one · 2011Article
- Sequential events in the irreversible thermal denaturation of human brain-type creatine kinase by spectroscopic methods.International journal of molecular sciences · 2010Article
- Dissecting the pretransitional conformational changes in aminoacylase I thermal denaturation.Biophysical journal · 2007Article
- Assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins.Biophysical journal · 2006Article
- Oligomerization and aggregation of bovine pancreatic ribonuclease A: characteristic events observed by FTIR spectroscopy.Biophysical journal · 2006Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Protein conformational changes may be associated with particular properties such as its function, transportation, assembly, tendency to aggregate, and potential cytotoxicity. In this research, the conformational change that is responsible for the fast destabilization and aggregation of rabbit muscle creatine kinase (EC 2.7.3.2) induced by heat was studied by intrinsic fluorescence and infrared spectroscopy. A pretransitional change of the tryptophan microenvironments was found from the intrinsic fluorescence spectra. A further analysis of the infrared spectra using quantitative second-derivative and two-dimensional correlation analysis indicated that the changes of the beta-sheet structures in the C-terminal domain and the loops occurred before the formation of intermolecular cross-beta-sheet structures and the unfolding of alpha-helices. These results suggested that the pretransitional conformational changes in the active site and the C-terminal domain might result in the modification of the domain-domain interactions and the formation of an inactive dimeric form that was prone to aggregate. Our results highlighted the fact that some minor conformational changes, which were usually negligible or undetectable by normal methods, might play a crucial role in protein stability and aggregation. Our results also suggested that the changes in domain-domain interactions, but not the dissociation of the dimer, might play a crucial role in the thermal denaturation and aggregation of this dimeric two-domain protein.
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