Peptostreptococcal protein

Mittermaier and Kay have carried out a detailed RDC-based study of Xi rotamer distributions for the B1 domain of peptostreptococcal protein... 

Residual dipolar couplings have been used by Mittermaier and Kay187 to probe the torsion angle dynamics of protein side-chains. Using the B1 domain of peptostreptococcal protein L, they show that the residual dipolar couplings can be used to distinguish static from mobile side-chains, and that the motions of most mobile side-chains can be adequately explained by rotamer-jump models. 

Kastem W, Sjobring U, Bjorck L Structure of peptostreptococcal protein L and identification of a repeated immunoglobulin light chain-binding domain. J Biol Chem 1992 267 12820-12825. 

Ricci S, Medaglini D, Marcotte H, Olsen A, Pozzi G, Bjorck L Immunoglobulin-binding domains of peptostreptococcal protein L enhance vaginal colonization of mice by Streptococcus gordonii. Microb Pathog 2001 30 229-235. 

The effects of mutations on the motions of side-chains in the B1 domain of peptostreptococcal protein L and in a pair of point mutants of the domain, F22I and A20V, have been investigated by Millet et a/. by the aid of methyl H spin relaxation rates and three-bond Cy-C(O), C -N and C -C6 couplings. It is noteworthy that the measurements of the relaxation rates provide information on a picosecond-nanosecond time scale, whereas J couplings span a wide range of time-scales. 

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See also in sourсe #XX -- [ ]

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