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Basic residue

Biosynthesis. Somatostatin exists in longer forms in several biological tissues (95,96). One of the longer forms, which has been isolated from porcine intestine, has been characterized as a 28-amino acid peptide (97). Somatostatin is derived from a precursor containing 116 amino acids (98,99). The precursor contains one copy of the somatostatin tetradecapeptide, which is contained within the sequence of the 28-amino acid peptide at the carboxy-terminal end of the precursor. The 28-amino acid somatostatin is preceded by a single Arg residue, while somatostatin 1-14 is preceded by a pair of basic residues. [Pg.203]

CCK has been detected in two principal forms, ie, the traditional 33-amino acid peptide, and an octapeptide CCK-8. The intestine produces mainly CCK-33 (133) and the brain produces mainly CCK-8 (132). The CCK precursor contains one copy of CCK-33 (133,134) this peptide is flanked on both ends with double basic residues, whereas CCK-8 is formed from CCK-33 by cleavage of a single basic residue. [Pg.204]

Group II consists of the enkephalins which come from the 267-aniino acid piecuisoi pro-enkephalin A [88402-54-4] (Fig. 2). This proteia contains four copies of Met-enkephalin, one copy of Leu-enkephalin, and the extended peptides Met-enkephalin-Arg -Phe (the last Met-enkephalin sequence ia Fig. 2) and Met-enkephalin-Arg -Gly -Leu (the fourth Met-enkephalin sequence ia Fig. 2) (25,26). AH of these products ate formed by trypsin-like cleavage between pairs of basic residues. The extended enkephalin peptides are further cleaved by carboxypeptidase E (27) to form authentic Met-enkephalin. [Pg.446]

The side of the p sheet that faces away from DNA is covered by two long a helices. One of these helices contains a number of basic residues from the middle segment of the polypeptide chain while the second helix is formed by the C-terminal residues. Residues from these two helices and from the short loop that joins the two motifs (red in Figure 9.4) are likely candidates for interactions with other subunits of the TFIID complex, and with specific transcription factors. [Pg.154]

Since the chemistry involved in the synthesis of these agents is self-evident, they are listed without comment in Table 1 below. The preparation of selected more complex basic residues is detailed in the section that follows. [Pg.123]

Margalit H. Fisher N. Ben-Sasson S.A. (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues // J. Biol. Chem V. 268. P.19228-19231. [Pg.219]

Most of the G-protein-coupled receptors are homologous with rhodopsin however, other quantitatively minor families as well as some individual receptors do not share any of the structural features common to the rhodopsin family (Figure 2.3). The most dominant of these are the glucagon/VIP/caldtonin receptor family, or family B (which has approximately 65 members), and the metabotropic glutamate receptor family, or family C (which has approximately 15 members), as well as the frizzled/smoothened family of receptors. Thus, the only structural feature that all G-protein-coupled receptors have in common is the seven-transmembrane helical bundle. Nevertheless, most non-rhodopsin-like receptors do have certain minor structural features in common with the rhodopsin-like receptors — for example, a disulfide bridge between the top of TM-III and the middle of extracellular loop-3, and a cluster of basic residues located just below TM-VI. [Pg.84]

The condensation reactions described above are unique in yet another sense. The conversion of an amine, a basic residue, to a neutral imide occurs with the simultaneous creation of a carboxylic acid nearby. In one synthetic event, an amine acts as the template and is converted into a structure that is the complement of an amine in size, shape and functionality. In this manner the triacid 15 shows high selectivity toward the parent triamine in binding experiments. Complementarity in binding is self-evident. Cyclodextrins for example, provide a hydrophobic inner surface complementary to structures such as benzenes, adamantanes and ferrocenes having appropriate shapes and sizes 12) (cf. 1). Complementary functionality has been harder to arrange in macrocycles the lone pairs of the oxygens of crown ethers and the 7t-surfaces of the cyclo-phanes are relatively inert13). Catalytically useful functionality such as carboxylic acids and their derivatives are available for the first time within these new molecular clefts. [Pg.200]

Tabb, D. L. Huang, Y. Wysocki, V. H. Yates, J. R. Influence of basic residue content on fragment ion peak intensities in low-energy collision-induced dissociation spectra of peptides. Anal. Chem. 2004, 76,1243-1248. [Pg.274]

The most important multiply charged polyatomic positive ions are compounds with two or more basic groups which when protonated lead to doubly or poly-charged ions. Typical examples are diamines such as the double protonated a, to alkyldiamines, H3N(CH2)pNH2+, and the most important class, the polyprotonated peptides and proteins, which have multiple basic residues. Charge reduction for these systems occurs through proton transfer from one of the protonated basic sites to a solvent molecule. Such a reaction is shown below for the monohydrate of a doubly protonated diamine ... [Pg.287]

Mary, S., Gomeza, J., Prezeau, L., Bockaert, J., and Pin, J.-P. (1998) A cluster of basic residues in the carboxyl-terminal tail of the short metabotropic glutamate receptor 1 variants impairs their coupling to phospholipase C. J. Biol. Chem. 273,425 132. [Pg.78]

Peptide length, as longer peptides have more groups where additional protons can be attached (basic residues). [Pg.180]

The second example contained two basic amino acids in the middle of the sequence, but closer to the C-terminus. The fragmentation spectrum contained a huge number of both C- and N-terminal peaks, with a high number of doubly charged ions, including both basic amino acids. The presence of basic residues caused a more balanced number of b- and y-ions but also made it very difficult to obtain fragments with bond cleavage near basic residues. [Pg.205]

Simple basic NLS SV40 type a stretch rich in basic residues and often in proline residues Importin /3/importin a family... [Pg.310]

The sequence features of presequences are well known typically they are from 20 to 80 residues long preferably contain basic residues, serine,... [Pg.313]


See other pages where Basic residue is mentioned: [Pg.188]    [Pg.204]    [Pg.88]    [Pg.616]    [Pg.620]    [Pg.32]    [Pg.1015]    [Pg.1026]    [Pg.233]    [Pg.280]    [Pg.225]    [Pg.225]    [Pg.339]    [Pg.225]    [Pg.189]    [Pg.25]    [Pg.40]    [Pg.310]    [Pg.424]    [Pg.183]    [Pg.153]    [Pg.424]    [Pg.324]    [Pg.324]    [Pg.416]    [Pg.253]    [Pg.74]    [Pg.356]    [Pg.263]    [Pg.16]    [Pg.310]    [Pg.314]    [Pg.314]    [Pg.28]    [Pg.766]   


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Amino acid residues, basic

Amino acid residues, basic functional groups

Cationic peptides, basic residues

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