Arginine chemical structure

Fig. 2.5.9 COSY spectra acquired at 600 MHz with an eight-coil probe along with the chemical structures of the compounds used. Each sample was a 10 mM solution in D20 loaded into the coil via the attached Teflon tubes, with the samples being (A) sucrose, (B) galactose, (C) arginine, (D) chloroquine, (E) cysteine, (F) caffeine, (G) fructose and (H)...

Otagiri et al. (22) used model peptides composed of arginine, proline, and phenylalanine to ascertain the relationship between bitter flavor and chemical structure. They reported that the presence of the hydrophobic amino acid at the C terminus and the basic amino acid at the N terminus brought about an increase in the bitterness of di- and tripeptides. They further noted a strong bitter taste when arginine was located next to proline and a synergistic effect in the peptides (Arg)r(Pro) ,-(Phe) (/ = 1,2 m, n = 1, 3) as the number of amino acids increased. Birch and Kemp (23) related the apparent specific volume of amino acids to taste. 

Arginine, 2D biosynthesis, 435 catabolism, 431 134 chemical structure, 20 plasma concentration, 465 Argininosuccinate lyase, 439 Acgininosuccinate synthase, 439 Aromatic amino acids, chemical structure, 19 Arsenate, 840 Artenosclcrosis, 357 Arteriovenous differences, 19 199 Artery, physiology, 359 Ascoitale... 

Fig. 5.3 Chemical structures of nitric oxide synthase inhibitors. Mj-nitro-L-arginine (L-NNA) (a) 5-[2-[(l-iminoethyl)amino]ethyl]-L-homocysteine (GW274150) (b) A-[3-(aminomethyl)benzyl] acetamidine (1,400 W) (c) AG-monomethyl-L-arginine (l-NMMA) (d) 7-nitroindazole (7-NI) (e) aminoguanidine (f) A6-iminoethyl-L-lysine (L-NIL) (g)...

FIGURE 8.20 Chemical structure of PEAs containing L-arginine amino acids with interesting features as nonviral transfer vector. 

This chapter describes their synthesis on a laboratory scale, some of the properties of noncommercial antimicrobial lipopeptidic surfactants derived from At -acyl arginine, and the relationships between antimicrobial function and the chemical structure of the hydrophobic and hydrophilic moieties. 

However, the overall rigid spatial structure is not the only feature important for a biological action. The chemical structure of arginine side chain is also crucial, as evinced from a dramatic loss of neurotoxic activity when both Arg are substituted either by lysine(20) or ornithine(18) residues. 

Fig. 4.14 NEXAFS C K-edge spectra and chemical structures of the six amino acids gUcyne (Gly), phenilalanine (Phe), histidine (His), tyrosine (Tyr), tryptophane (Trp) and arginine (Arg). (Reprinted from Boese et al. [41], Copyright (2009), with permission from Elsevier)...

Fig. 37.8 Chemical structure of the p-phosphonato-calix[4]arene (a) and suggested binding mode of the p-phosphonate-calix[4]arene embedded in a stearic acid monolayer with arginine residues of basic proteins dissolved in the aqueous subphase (b) (Reproduced with permission from Ref. [53], Copyright 2005, American Chemical Society)...

FIGURE 15.6 Chemical structure of L-arginine showing guanidnium, carboxyl, and amine groups. 

The envelope proteins shown in Fig. 8 are double labeled with PH]arginine and [ C]histidine. As can be seen from the profiles, both peak 11 and the shoulder peak (shown by an arrow), in contrast to all other peaks, have an extremely low content of histidine. This provides evidence that the peak 11 protein and the protein at the shoulder are composed of the same polypeptide, which lacks histidine residues. In the next section, more definitive proof, including the chemical structures of the bound and free forms, will be discussed. 

Neurotoxins present in sea snake venoms are summarized. All sea snake venoms are extremely toxic, with low LD5Q values. Most sea snake neurotoxins consist of only 60-62 amino acid residues with 4 disulOde bonds, while some consist of 70 amino acids with 5 disulfide bonds. The origin of toxicity is due to the attachment of 2 neurotoxin molecules to 2 a subunits of an acetylcholine receptor that is composed of a2 6 subunits. The complete structure of several of the sea snake neurotoxins have been worked out. Through chemical modification studies the invariant tryptophan and tyrosine residues of post-synaptic neurotoxins were shown to be of a critical nature to the toxicity function of the molecule. Lysine and arginine are also believed to be important. Other marine vertebrate venoms are not well known. 

---