Structural characterisation of the natively unfolded enterocin EJ97
نویسندگان
چکیده
منابع مشابه
Natively unfolded proteins.
It is now clear that a significant fraction of eukaryotic genomes encode proteins with substantial regions of disordered structure. In spite of the lack of structure, these proteins nevertheless are functional; many are involved in critical steps of the cell cycle and regulatory processes. In general, intrinsically disordered proteins interact with a target ligand (often DNA) and undergo a stru...
متن کاملNatively unfolded proteins: An overview
Proteins with wholly or partly denatured structures in vivo are called intrinsically disordered or natively unfolded proteins (NUPs). Functional importance of NUPs was revealed by NMR studies as first reviewed by P. Wright in 1999. Since then, computational analyses on NUPs have also been intensively carried out to predict that approximately one third of eukaryotic proteins are NUPs. I will sta...
متن کاملThe genes coding for enterocin EJ97 production by Enterococcus faecalis EJ97 are located on a conjugative plasmid.
Enterococcus faecalis EJ97 produces a cationic bacteriocin (enterocin EJ97) of low molecular mass (5,327.7 Da). The complete amino acid sequence of enterocin EJ97 was elucidated after automated microsequencing of oligopeptides generated by endoproteinase GluC digestion and cyanogen bromide treatment. Transfer of the 60-kb conjugative plasmid pEJ97 from the bacteriocinogenic strain E. faecalis E...
متن کاملNatively unfolded regions of the vertebrate fibrinogen molecule.
Although it has long been realized that a large portion of the fibrinogen alpha chain has little if any defined structure, the physiological significance of this flexible appendage remains mysterious.
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 2010
ISSN: 1741-0134,1741-0126
DOI: 10.1093/protein/gzq020