Journal ArticleDOI
Thermodynamic study of domain organization in troponin C and calmodulin.
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TLDR
It is shown by thermodynamic analysis of the experimentally determined excess heat capacity function that the four calcium-binding domains in these two related proteins are not integrated into a single co-operative system, as would be the case if they formed a common hydrophobic core in the molecule, but still interact with each other in a very specific way.About:
This article is published in Journal of Molecular Biology.The article was published on 1985-02-20. It has received 146 citations till now. The article focuses on the topics: Troponin C & Calmodulin.read more
Citations
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Book ChapterDOI
Scanning microcalorimetry in studying temperature-induced changes in proteins.
Peter L. Privalov,S. A. Potekhin +1 more
Journal ArticleDOI
Solution structure of calcium-free calmodulin.
TL;DR: The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings.
Journal ArticleDOI
Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
TL;DR: It is shown that the proposed model may be considered as being one particular case of that proposed by Lumry and Eyring, where N in equilibrium D----I is the native state, D the unfolded one, and I a final state, irreversibly arrived at from D.
Journal ArticleDOI
Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.
Michael W. Pantoliano,Marc Whitlow,Jay F. Wood,Steven Witt Dodd,Karl D. Hardman,Michele L. Rollence,Philip N. Bryan +6 more
TL;DR: Thermodynamic stability was shown to be related to resistance to irreversible inactivation, which included elevated temperatures or extreme alkalinity, and under these denaturing conditions, the rate of inactivation of the combination variant is approximately 300 times slower than that of the wild-type subtilisin BPN'.
Journal ArticleDOI
Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation.
TL;DR: This work obtains numerical solutions for N, U, and D as a function of temperature for this model and derive profiles of excess specific heat (Cp) in terms of the reduced variables v/ki and k1/k3, where v is the scan rate.
References
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Journal ArticleDOI
Calmodulin plays a pivotal role in cellular regulation
TL;DR: The role of calcium ions (Ca2+) in cell function is beginning to be unraveled at the molecular level as a result of recent research on calcium-binding proteins and particularly on calmodulin.
Book ChapterDOI
Stability of Proteins Small Globular Proteins
TL;DR: The chapter discusses the stability of proteins and presents the results obtained on small compact globular proteins, which represent one single cooperative system, and the temperature-induced changes in protein, denaturational and predenaturational changes inprotein, thermodynamics of protein unfolding, and thermodynamic properties of protein.
Book ChapterDOI
Stability of proteins. Proteins which do not present a single cooperative system
TL;DR: The practical importance of thermodynamic studies of protein stability—that is, its importance not only for understanding the principles of organization of these molecules, but just for obtaining structural information on the domain level is emphasized.
Journal ArticleDOI
Structure and evolution of calcium-modulated proteins.
TL;DR: The intracellular functions of calcium are best understood in terms of calcium's functioning as a second messenger, and this line of thought leads to a suggestion of the evolutionary reason for the choice of calcium as the sole inorganic second messenger.