Document Detail


Relative stability of human centrins and its relationship to calcium binding.
MedLine Citation:
PMID:  23346931     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Centrins are calcium binding proteins that belong to the EF-hand superfamily with diverse biological functions. Herein we present the first systematic study that establishes the relative stability of related centrins via complementary biophysical techniques. Our results define the stepwise molecular behavior of human centrins by two-dimensional infrared (2D IR) correlation spectroscopy, the change in heat capacity and enthalpy of denaturation by differential scanning calorimetry, and the relative stability of the helical regions of centrins by circular dichroism. More importantly, 2D IR correlation spectroscopy provides unique information about the similarities and differences in dynamics between these related proteins. The thermally induced molecular behavior of human centrins can be used to predict biological target interactions that have a relative dependence on calcium affinity. This information is essential for understanding why certain isoforms may be used to rescue a phenotype and therefore also for explaining the different functions these proteins may have in vivo. Furthermore, this comparative approach can be applied to the study of recombinant therapeutic protein candidates for the treatment of disease states.
Authors:
Belinda Pastrana-Ríos; Myrna Reyes; Jessica De Orbeta; Verónica Meza; Daniel Narváez; Ana María Gómez; Aslin Rodríguez Nassif; Ruth Almodovar; Adalberto Díaz Casas; José Robles; Ana María Ortiz; Lizbeth Irizarry; Melissa Campbell; Mara Colón
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-02-06
Journal Detail:
Title:  Biochemistry     Volume:  52     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-19     Completed Date:  2013-04-26     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1236-48     Citation Subset:  IM    
Affiliation:
Protein Research Center, University of Puerto Rico, Mayagüez Campus, Mayagüez, Puerto Rico 00681-9019, USA. belinda@hpcf.upr.edu
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Calcium / metabolism*
Calcium-Binding Proteins / chemistry*,  metabolism
Calorimetry, Differential Scanning
Cell Cycle Proteins / chemistry*,  metabolism
Circular Dichroism
Humans
Molecular Sequence Data
Protein Conformation
Protein Denaturation
Spectroscopy, Fourier Transform Infrared
Spectrum Analysis / methods
Grant Support
ID/Acronym/Agency:
R25 GM088023/GM/NIGMS NIH HHS; S06GM08103/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/CETN2 protein, human; 0/CETN3 protein, human; 0/Calcium-Binding Proteins; 0/Cell Cycle Proteins; 0/centrin 1 protein, human; 7440-70-2/Calcium
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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