Biomaterial Database

[Letter: Temperature dependence of myosin fluorescence]. 1975

N V Medvedeva, and E K Ruuge

It was shown that an increase of temperature (from 0 to 37 degrees C) did not affect the maximum position of the myosin fluorescence spectrum and relative contribution of tyrosine to fluorescence intensity. The spectral band width increases to 2-3 nm. The I (t-o) relationship permits us to sugges that the temperature change causes structural changes of myosine molecules.

UI	MeSH Term	Description	Entries
D008968	Molecular Conformation	The characteristic three-dimensional shape of a molecule.	Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D009218	Myosins	A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.	Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D013050	Spectrometry, Fluorescence	Measurement of the intensity and quality of fluorescence.	Fluorescence Spectrophotometry,Fluorescence Spectroscopy,Spectrofluorometry,Fluorescence Spectrometry,Spectrophotometry, Fluorescence,Spectroscopy, Fluorescence
D013696	Temperature	The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.	Temperatures

Related Publications

N V Medvedeva, and E K Ruuge

Temperature dependence of collagen fluorescence.

April 2006, Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology,

N V Medvedeva, and E K Ruuge

Temperature dependence of myosin-II tail fragment assembly.

January 2008, Journal of muscle research and cell motility,

N V Medvedeva, and E K Ruuge

Temperature Dependence of Dissolved Organic Matter Fluorescence.

August 2018, Environmental science & technology,

N V Medvedeva, and E K Ruuge

Temperature dependence of the fluorescence properties of curcumin.

October 2011, The journal of physical chemistry. A,

N V Medvedeva, and E K Ruuge

Letter: Temperature dependence of human T-cells rosettes.

October 1973, Lancet (London, England),