Biomaterial Database

Ca2+-induced conformational changes in the troponin complex detected by crosslinking. 1980

N B Gusev, and P Friedrich

In an attempt to detect Ca2+-induced conformational changes by crosslinking, rabbit muscle troponin complex was reacted with the bifunctional reagents 1,3-difluoro-4,6-dinitrobenzene, 4,4'-difluoro-3,3'-dinitrodiphenylsulfone and dimethyl suberimidate under various conditions and the products were analyzed by dodecyl sulfate gel electrophoresis. In the absence of divalent cations, with the two aromatic reagents at a low reagent/protein ratio, the main cross-link products were troponin T-I and I-C. With dimethyl suberimidate the only major crosslink product was conjugate T-I. Ca2+, alone as well as in the presence of Mg2+, prevented the formation of I-C crosslinks with both aromatic reagents, but it did not affect crosslinking with dimethyl suberimidate. Ca2+ also decreased the number of NH2 groups of troponin that are highly reactive towards 2,4,6-trinitrobenzene sulfonate. Both effects of Ca2+ can be interpreted in terms of a conformational change in the troponin complex elicited by the binding of the specific divalent cation.

UI	MeSH Term	Description	Entries
D008433	Mathematics	The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)	Mathematic
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009994	Osmolar Concentration	The concentration of osmotically active particles in solution expressed in terms of osmoles of solute per liter of solution. Osmolality is expressed in terms of osmoles of solute per kilogram of solvent.	Ionic Strength,Osmolality,Osmolarity,Concentration, Osmolar,Concentrations, Osmolar,Ionic Strengths,Osmolalities,Osmolar Concentrations,Osmolarities,Strength, Ionic,Strengths, Ionic
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
D011817	Rabbits	A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes.	Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
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
D003432	Cross-Linking Reagents	Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.	Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D004120	Dimethyl Suberimidate	The methyl imidoester of suberic acid used to produce cross links in proteins. Each end of the imidoester will react with an amino group in the protein molecule to form an amidine.	Bismethyl Suberimidate,Dimethylsuberimidate,Suberimidate, Bismethyl,Suberimidate, Dimethyl
D004139	Dinitrofluorobenzene	Irritants and reagents for labeling terminal amino acid groups.	DNFB,Fluorodinitrobenzene,1-Fluoro-2,4-dinitrobenzene,1 Fluoro 2,4 dinitrobenzene