Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Tyrosine uppers

In the high resolution structure, Tyr 91 and 93 are indeed buried deep in the hydrophobic area between the back wall of the pocket and the rear edge of the nuclease molecule. Tyrosine 27, which is more resistant to nitration in the inhibited nuclease, is probably hydrogen bonded to the carboxylate of Glu 10, partially shielded by the methylene chain of Lys 28, and, most importantly, at the rear upper right... [Pg.173]

Figure 9.33 Representative chromatogram of tyrosine (T), tyrosylglycine (T-G) and tyrosylglycylglycine (T-G-G) standards. Upper (HPLC-UV) and [HPLC-electro-chemical detection (ED)] chromatograms shows the separation of 55 ng of T-G-G (1), 70 ng of T-G (2), and 35 ng of T (3). Analytes were detected at 205 nm (0.1 A) and + 1.25 V oxidation potential (100 nA). (From Mousa and Couri, 1983.)... Figure 9.33 Representative chromatogram of tyrosine (T), tyrosylglycine (T-G) and tyrosylglycylglycine (T-G-G) standards. Upper (HPLC-UV) and [HPLC-electro-chemical detection (ED)] chromatograms shows the separation of 55 ng of T-G-G (1), 70 ng of T-G (2), and 35 ng of T (3). Analytes were detected at 205 nm (0.1 A) and + 1.25 V oxidation potential (100 nA). (From Mousa and Couri, 1983.)...
PYY is a 36-amino-acid peptide originally isolated from porcine upper intestine by Tatemoto et al. (26, 27). It contains an A-terminal tyrosine and a C-terminal tyrosine amide and therefore is named peptide YY. It has a high degree of sequence homology (70%) with neuropeptide Y, and it strongly inhibits pancreatic exocrine secretion and jejunal and colonic motility as well as causes vasoconstriction. [Pg.2189]

Figure 4. N-acetyl phenylalanyl tyrosine in the crystal (upper) and minimized... Figure 4. N-acetyl phenylalanyl tyrosine in the crystal (upper) and minimized...
Figure 5.49. Sections from the DQF-COSY spectrum of the pentapeptide Leu-enkephalin 5.4. The 2D crosspeaks and the f2 ID trace taken through these correspond to correlations within the tyrosine (Y) residue. The upper trace is taken from the conventional ID spectrum in which the P-proton resonances partially overlap with those of phenylalanine (F). The original 2D data had an f2 resolution of 1.8 Hz/pt but the ID trace was treated as described in the text to yield a final resolution of 0.4 Hz/pt. Figure 5.49. Sections from the DQF-COSY spectrum of the pentapeptide Leu-enkephalin 5.4. The 2D crosspeaks and the f2 ID trace taken through these correspond to correlations within the tyrosine (Y) residue. The upper trace is taken from the conventional ID spectrum in which the P-proton resonances partially overlap with those of phenylalanine (F). The original 2D data had an f2 resolution of 1.8 Hz/pt but the ID trace was treated as described in the text to yield a final resolution of 0.4 Hz/pt.
Figure 14 Signal improvement by multi-flash CIDNP experiments with storage and accumulation in the spin system. Delay At (see, Figure 13) between laser flash and sampling rf pulse, 0 jis. Bottom trace absorptive doublet and emissive AB spin system of 3-fluoro-DL-tyrosine. Top trace multiplet effect in S-NADH. The number of flashes accumulated before one acquisition is given at the upper spectra, 1 denoting the control experiment with the standard sequence of Figure 9. It is seen that neither multiplet signals nor CIDNP multiplet effects are distorted by the method. Further explanation, see text. Adapted from Ref. 75 with permission copyright (2006) Taylor Francis Ltd, http / www.tandfco.uk/journals. Figure 14 Signal improvement by multi-flash CIDNP experiments with storage and accumulation in the spin system. Delay At (see, Figure 13) between laser flash and sampling rf pulse, 0 jis. Bottom trace absorptive doublet and emissive AB spin system of 3-fluoro-DL-tyrosine. Top trace multiplet effect in S-NADH. The number of flashes accumulated before one acquisition is given at the upper spectra, 1 denoting the control experiment with the standard sequence of Figure 9. It is seen that neither multiplet signals nor CIDNP multiplet effects are distorted by the method. Further explanation, see text. Adapted from Ref. 75 with permission copyright (2006) Taylor Francis Ltd, http / www.tandfco.uk/journals.
Figure 5.21. Upper Aromatic region of 500 MHz H-NMR spectrum of the complex between 2,4-diaminopyrimidine and selectively deuterated dihydrofolate reductase, in which the only aromatic protons remaining were the 2 6 -protons of the five tyrosine residues. Lower Difference spectrum showing the NOE effects observed on irradiating resonance in this sample. Figure 5.21. Upper Aromatic region of 500 MHz H-NMR spectrum of the complex between 2,4-diaminopyrimidine and selectively deuterated dihydrofolate reductase, in which the only aromatic protons remaining were the 2 6 -protons of the five tyrosine residues. Lower Difference spectrum showing the NOE effects observed on irradiating resonance in this sample.
Figure 12 (a) Structure of tyrosine ethyl ester showing the separation between the labeled carbons, (b) Calculated and experimental evolution of the difference polarization for the n = 1 rotational resonance in tyrosine ethyl ester at 9.5 T and (aJlTT = 9.400 kHz [92]. The solid curve is calculated for 0.505 nm, and the upper and lower dotted curves for 0.555 and 0.455 nm, respectively. [Pg.380]

HV, healthy volunteers M, males F, females XO, crossover SD, single dose MD, multiple dose T, therapeutic dose ST, supratherapeutic dose P, placebo M, moxifloxacin, single oral dose of 400 mg nested XO, nested crossover comparison for moxifloxacin lacebo within a parallel group study T + keto, therapeutic dose concomitant with ketoconazole. TKI, tyrosine kinase inhibitor, Cl, confidence interval LB, lower bound. Negative upper bound of Cl < 10 ms for doses studied... [Pg.441]

Fig. 129. Difference spectra of tyrosine solutions (0.0009 to 0.0012 M). Upper in 7.2 M LiBr, 7.0 M LiCl, 5.1 M NaBr, 4.0 M NaCl, and 4.1 M Nal. Lower in 6 M urea and in a concentrated sucrose solution whose refractive index was approximately equal to that of the 6 M urea (Bigelow and Geschwind, 1960). Fig. 129. Difference spectra of tyrosine solutions (0.0009 to 0.0012 M). Upper in 7.2 M LiBr, 7.0 M LiCl, 5.1 M NaBr, 4.0 M NaCl, and 4.1 M Nal. Lower in 6 M urea and in a concentrated sucrose solution whose refractive index was approximately equal to that of the 6 M urea (Bigelow and Geschwind, 1960).
Using this procedure. Red wine et al. obtained an upper limit for the temperature of 10-16 K for their 22-pole ion trap, consistent with what we measured in our 22-pole trap [46] as well as in a newly constructed cold octupole trap. In contrast, the 3-D quadrupole ion trap employed by Choi et al. attained temperatures of 45-54 K for protonated tyrosine [138], which is likely to reflect RF heating of the ions. [Pg.70]

FIGURE 14.3 Structure of ApS-16 and a-syn34—45. In the upper panel, the basic residues at each end of the peptides are in red and the central tyrosine in blue. The position of His-13/His-14 (Ap) and Ser-42/Lys-43 (a-synuclein) is framed in yellow. The minimized structures of both peptides are shown in the lower panel. (Adapted from Yahi and... [Pg.342]


See other pages where Tyrosine uppers is mentioned: [Pg.930]    [Pg.110]    [Pg.20]    [Pg.215]    [Pg.1749]    [Pg.18]    [Pg.182]    [Pg.930]    [Pg.347]    [Pg.237]    [Pg.146]    [Pg.301]    [Pg.307]    [Pg.116]    [Pg.166]    [Pg.64]    [Pg.64]    [Pg.149]    [Pg.365]    [Pg.365]    [Pg.369]    [Pg.191]    [Pg.276]    [Pg.456]    [Pg.836]    [Pg.815]    [Pg.83]    [Pg.456]    [Pg.514]    [Pg.575]    [Pg.862]    [Pg.82]    [Pg.189]    [Pg.348]    [Pg.264]    [Pg.424]    [Pg.740]    [Pg.269]   
See also in sourсe #XX -- [ Pg.96 ]




SEARCH



© 2024 chempedia.info