Carboxylate terminus

EIectrosta.tlcs. Electrostatic interactions, such as salt bridges, result from the electrostatic attraction that occurs between oppositely charged molecules. These usually involve a single cation, eg, the side chain of Lys or Arg, or the amino terminus, etc, interacting with a single anion, eg, the side chain of Glu or Asp, or the carboxyl terminus, etc. This attractive force is iaversely proportional to the distance between the charges and the dielectric constant of the solvent, as described by Coulomb s law. 

Molecules of interest that contain free amino groups can be coupled in aqueous solution to /S-poIy(L-malate) as amides using carbodiimides such as the water-soluble l-ethyl-3(3-dimethyIaminopropyl)carbodiimide hydrochloride (EDC) [2,12,20,21]. By this method, the molecules are attached randomly. A selective amide bond formation at the carboxylate terminus can be achieved... 

Disulfide bridges formation ChEs contain 8-10 cysteines six of these form three internal disulfide bridges. The cysteine that is located four amino acids upstream the carboxyl terminus forms a disulfide bridge with a cysteine of an identical subunit, creating an interchain disulfide bridge, which stabilizes the dimeric structure. 

S-prenyl (famesyl) T T T S-Cys Cysteine at/near carboxyl-terminus... 

The digestion of the protein, after heme removal, using Glu-C endoproteinase was also carried out. This enzyme cleaves the polypeptide backbone on the carboxyl terminus of a glutamic acid residue and in this case yielded twelve chromatographic responses. Despite two of these arising from unresolved components, molecular weight information was obtained from 15 polypeptides, one of which was the intact protein, covering the complete sequence, as shown in Table 5.10. 

The resulting model (Figure 5.12) 1"1 takes many of these considerations into account (i) most contacts with transferrin involve the Ci domain, with additional contributions from the Ni domain, particularly near to its carboxyl terminus (ii) the N2 and C2 domains of transferrin have only minor interactions with the receptor ... 

Zhu X, Wang C, Cheng Z et al. The carboxyl terminus of mouse d-opioid receptor is not required for agonist-dependent activation. Biochem Biophys Res Commun 1997 232, 513-516. 

The KKXX sequence is present at the carboxyl terminus of ER membrane proteins, while the H/KDEL is present in soluble ER proteins, such as the aforementioned... 

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