Amino acid residues, basic

Valinomycin has a cyclic structure resembling a peptide chain containing 12 amino acid residues basically it is a four-unit structure that is repeated three times ... 

Fig. 3.1. Posttranslational modifications of Ras superfamily small GTPases in which both prenylation and C-terminal phosphorylation have been demonstrated. The sequences of the hypervariable (membrane targeting) domain (HVD) of each such GTPase are shown. Known phosphorylation sites are bolded and shown in red numbers are amino acid residues. Basic residues (with a positive charge) are shown in blue. Responsible kinases are indicated. S, serine T, threonine Y, tyrosine.

Fig. 1. Schematic drawing of precursors for selected brain oligopeptides. Shaded areas represent the location of sequences of active peptide products which are normally cleaved by trypsin-like enzymes acting on double-basic amino acid residues. Precursors are not necessarily drawn to scale, (a) CRF precursor (b) proopiomelanocortin (POMC) (c) P-protachykinin (d) proenkephalin A (e) CGRP precursor (f) preprodynorphin, ie, preproenkephalin B. Terms are...

Biosynthesis. Two closely related genes encode the three mammalian tachykinins. The preprotachykinin A gene encodes both substance P and substance K, while the preprotachykinin B gene encodes neuromedin K (45—47). The active sequences are flanked by the usual double-basic amino acid residues, and the carboxy-terrninal amino acid is a glycine residue which is decarboxylated to an amide. As with most neuropeptide precursors, intermediates in peptide processing can be detected, but their biological activities are not clear (ca 1994). 

CGRP has a wide distribution in the nervous system (19) and was the first peptide to be localized to motoneurons (124). It is also found in primary sensory neurons where it is colocalized with substance P (125). CGRP is derived from a precursor stmcturaHy related to the calcitonin precursor. The latter precursor produces two products, calcitonin itself and katacalcin, while the CGRP precursor produces one copy of CGRP (123). Like other peptides, CGRP is cleaved from its precursor by tryptic breakdown between double basic amino acid residues. 

Histone H3 Histones are DNA-binding proteins found in chromosomes 135 amino acid residues. Note die very basic nature of this protein dne to its abmidance of Arg and Lys residues. It also lacks tryptophan. 

Phenols with an appropriate leaving group in the benzylic position such as fluoride may form QMs by spontaneous hydrolysis, possibly catalyzed by a basic amino acid residue as shown in Scheme 10.2c. Evidence for this process was obtained with 4-(fluoromethyl)phenyl phosphate involving initial enzymatic hydrolysis of the phosphate followed by nonenzymatic formation of a QM.11 Similarly, several lines of evidence demonstrate nonenzymatic QM formation from 4-trifluoromethylphenol under physiologic conditions.12... 

Although the order of affinity of PF-4 for different glycosaminogly-cans, and dissociation of their complexes with salts, are typical of nonspecific, electrostatic interactions, PF-4 is not strictly a cationic protein.452 It is probable that heparin binds to clusters of basic amino acids (two lysine pairs) near the carboxyl terminal of a polypeptide chain that has an overall preponderance of acidic amino acid residues.457 High-molecular-weight heparin species can bind two PF-4 molecules, with formation of complexes 10 to 100 times as strong as those with antithrombin.217... 

Figure 19.1 A schematic view of the common formaldehyde-induced modifications in proteins. Reactive methylol adducts are formed in the initial reaction between formaldehyde and cysteine or the amino groups of basic amino acid residues. The methylol adduct can subsequently undergo a dehydration reaction to form a Schiff s base. Adducted residues can undergo a second reaction to form methylene bridges or can convert to the ethoxymethyl adduct after the ethanol dehydration step.

At the time the hormone is introduced into the LBD (Fig. 1.4), a conformational change is produced in the three-dimensional structure of the receptor, a change that is key to the subsequent steps in hormonal action. This change is produced by a few contacts (between 6 or 7 and 15) of the receptor s amino acids with related groups from the hormone s structure. Some basic amino acid residues, particularly from arginine, which are preserved virtually intact among receptors, are critical in the execution of this function (Quingley et al. 1995). 

There are several subfamilies of PKs, which either require Ca2+, diacyl glycerol or phorbol esters or extracellular agonists for activation. Four major groups of PKs are distinguished. Basic amino acid-directed kinases (PKA, PKB, PKC) phophorylate serine/threonine around such amino acid residues. PKA is activat-... 

Most of the research performed in this field is based on tryptic peptides. As discussed earlier, such peptides contain basic amino acid residues on their C-terminus, which causes formation of the high intensity C-terminal ion series, mostly y-ions. In such peptides the N-terminal ions have lower intensity and do not provide important sequence information. Introduction of a highly basic group, such as dimethylalkyl-ammonium acetyl (DMAA) or tra(2,4,6-trimcthoxyphcnyl)phosphonium acetate into... 

DABCO = l,4-diazabicyclo[2,2,2]octane (triethylene diamine) (22) is a moderately basic amine, removable by sublimation, that causes enantiomeriza-tion of amino acid residues that have been reacted to form Schiff s bases (RR C=NCHR2CO-). 

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