Biomaterial Database

Calcium-induced conformational changes in a cyanogen bromide fragment of troponin C that contains one of the binding sites. 1978

B Nagy, and J D Potter, and J Gergely

The increase observed in alpha helix from 20 to 38%, the spectral red shift of the absorption bands of the side chain chromophores, the increase of phenylalanine side chain optical activity and a decrease of cysteinyl side chain reactivity with 5,5'-dithiobis(2-nitrobenzoic acid) are consistent with a coil to helix change in the segment containing Cys-98 and Phe-99 and 102 when the CB9 fragment of troponin C (TnC) with an intact binding site III binds Ca2+. Since similar spectrophotometric observations have been made on the whole molecule the data with CB9 confirm our previous suggestion that binding site III of TnC is one of the strong binding sites for Ca2+. The estimate of the binding constant of Ca2+ for CB9 is about 2 orders of magnitude lower than in whole TnC, indicating further stabilization in the intact molecule.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D009124	Muscle Proteins	The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.	Muscle Protein,Protein, Muscle,Proteins, Muscle
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D002118	Calcium	A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.	Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002942	Circular Dichroism	A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D013056	Spectrophotometry, Ultraviolet	Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Ultraviolet Spectrophotometry
D014336	Troponin	One of the minor protein components of skeletal and cardiac muscles. It functions as the calcium-binding component in a complex with BETA-TROPOMYOSIN; ACTIN; and MYOSIN and confers calcium sensitivity to the cross-linked actin and myosin filaments. Troponin itself is a complex of three regulatory proteins (TROPONIN C; TROPONIN I; and TROPONIN T).	Troponin Complex,Troponins