Rabbit muscle conformational changes

Wang S, Wang X, Shi W et al (2008) Detection of local polarity and conformational changes at the active site of rabbit muscle creatine kinase with a new arginine-specific fluorescent probe. Biochim Biophys Acta 1784 415 -22... 

Tsuda, S., Ogura, K., Hasegawa, Y., Vagi, K., and Hikichi, K. (1990). H NMR study of rabbit skeletal muscle troponin C Mgf -Induced conformational change. Biochemistry 29, 4951-4958. 

The role of sulfhydryl groups in phosphorylase activity is not yet known. Modification with p-chloromercuribenzoate certainly causes loss of activity, but it is uncertain whether die sulfhydryl groups form a part of the active center, or are more important for the maintenance of the active conformation of the protein molecule. The second possibility seems the more likely, as p-chloromercuribenzoate causes rabbit-muscle phosphorylase to split up into subunits. Also, the inhibition by this reagent is not parallel to mercaptide formation, and adenosine 5 -phosphate (which causes changes in the conformation of the enzyme) protects against the inhibition. Unmodified sulfhydryl groups are believed to be important for the binding of adenosine 5 -phosphate. ... 

Frieden, C, (1982). The Mg -Induced conformational change in rabbit skeletal muscle C actin, /. Bio . Chem. 157, 2882-2886. 

Nixon GF, lizuka K, Haystead CM, Haystead TA, Somlyo AP, Somlyo AV (1995) Phosphorylation of caldesmon by mitogen-activated protein kinase with no effect on Ca sensitivity in rabbit smooth muscle. J Physiol (Lond) 487 283-289 Noda S, Ito M, Watanabe S, Takahashi K, Maruyama K (1992) Conformational changes of actin induced by calponin. Biochem Biophys Res Commun 1992 May 29 185(l) 481-487... 

Calsequestrin is a calcium-storage protein found in the sacroplasmic reticulum, which binds about 50 calcium ions per monomer (molecular weight 40 000) with binding constants in the range 103-105 dm3 mol. Release and uptake of Ca2+ during muscle contradion and relaxation involve this store. Calsequestrin from rabbit skeletal muscle has a random coil conformation in the absence of calcium. Binding of Ca2+ is associated with a change to a more compact structure.267... 

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