| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| S Aravinda, N Shamala, A Pramanik, C Das, P Balara. An unusual C-H...O hydrogen bond mediated reversal of polypeptide chain direction in a synthetic peptide helix. Biochemical and biophysical research communications. vol 273. issue 3. 2000-09-08. PMID:10891350. |
the crystal structure of the decapeptide boc-leu-aib-val-ala-leu-aib-val-(d)ala-(d)leu-aib-ome reveals a helical segment spanning residues 1-7 and helix termination by formation of a schellman motif, generated by (d)ala(8) adopting the left-handed helical (alpha(l)) conformation. |
2000-09-08 |
2023-08-12 |
Not clear |
| S Aravinda, N Shamala, A Pramanik, C Das, P Balara. An unusual C-H...O hydrogen bond mediated reversal of polypeptide chain direction in a synthetic peptide helix. Biochemical and biophysical research communications. vol 273. issue 3. 2000-09-08. PMID:10891350. |
the extended conformation at (d)leu(9) results in a compact folded structure, stabilized by a potentially strong c-h. o hydrogen bond between ala(4) c(alpha)h and (d)leu(9) co. |
2000-09-08 |
2023-08-12 |
Not clear |
| S Aravinda, N Shamala, A Pramanik, C Das, P Balara. An unusual C-H...O hydrogen bond mediated reversal of polypeptide chain direction in a synthetic peptide helix. Biochemical and biophysical research communications. vol 273. issue 3. 2000-09-08. PMID:10891350. |
the parameters for c-h. o interaction are ala(4) c(alpha)h. o=c (d)leu(9) distance 3.27 a, c(alpha)-h. o angle 176 degrees, and o. h(alpha) distance 2.29 a. |
2000-09-08 |
2023-08-12 |
Not clear |
| S Liu, M H Ginsber. Paxillin binding to a conserved sequence motif in the alpha 4 integrin cytoplasmic domain. The Journal of biological chemistry. vol 275. issue 30. 2000-08-31. PMID:10781578. |
the role of these residues was confirmed by introducing these ala substitutions into the full-length alpha(4) tail sequence. |
2000-08-31 |
2023-08-12 |
xenopus_laevis |
| A P Mould, J A Askari, M J Humphrie. Molecular basis of ligand recognition by integrin alpha 5beta 1. I. Specificity of ligand binding is determined by amino acid sequences in the second and third NH2-terminal repeats of the alpha subunit. The Journal of biological chemistry. vol 275. issue 27. 2000-08-16. PMID:10764748. |
our results demonstrate that: (a) the first three nh(2)-terminal repeats contain the amino acid sequences that determine ligand binding specificity and the same repeats include the epitopes of function blocking anti-alpha subunit mabs; (b) the divalent cation-binding sites (in repeats 4-7) do not confer alpha(5)beta(1)- or alpha(v)beta(1)-specific ligand recognition; (c) amino acid residues ala(107)-tyr(226) of alpha(5) (corresponding approximately to repeats 2 and 3) are sufficient to change all the ligand binding properties of alpha(v)beta(1) to those of alpha(5)beta(1); (d) swapping a small part of a predicted loop region of alpha(v) with the corresponding region of alpha(5) (asp(154)-ala(159)) is sufficient to confer selectivity for rgdgw and the ability to recognize rretawa. |
2000-08-16 |
2023-08-12 |
Not clear |
| P A Stevens, N Bevan, S Rees, G Milliga. Resolution of inverse agonist-induced up-regulation from constitutive activity of mutants of the alpha(1b)-adrenoceptor. Molecular pharmacology. vol 58. issue 2. 2000-08-16. PMID:10908313. |
constitutively active forms of the hamster alpha(1b)-adrenoceptor can be produced from the point mutations asp(142)ala or ala(293)glu or exchange of a small segment of the third intracellular loop with the equivalent region of the beta(2)-adrenoceptor. |
2000-08-16 |
2023-08-12 |
Not clear |
| P A Stevens, N Bevan, S Rees, G Milliga. Resolution of inverse agonist-induced up-regulation from constitutive activity of mutants of the alpha(1b)-adrenoceptor. Molecular pharmacology. vol 58. issue 2. 2000-08-16. PMID:10908313. |
in contrast, both the asp(142)ala and ala(293)glu forms of the alpha(1b)-adrenoceptor-gfp were located predominantly at the plasma membrane. |
2000-08-16 |
2023-08-12 |
Not clear |
| A H Mawjood, G Miyazaki, R Kaneko, Y Wada, K Ima. Site-directed mutagenesis in hemoglobin: test of functional homology of the F9 amino acid residues of hemoglobin alpha and beta chains. Protein engineering. vol 13. issue 2. 2000-05-18. PMID:10708650. |
to clarify the role of this residue and its functional homology to f9(88) of the alpha chain, we measured oxygen equilibrium curves, uv-region derivative spectra, soret-band absorption spectra, the number of titratable -sh groups with p-mercuribenzoate and the rate of reaction of these groups with 4, 4'-dipyridine disulfide for three recombinant mutant hbs with single amino acid substitutions: ala-->cys at 88alpha (rhb a88alphac), cys-->ala at 93beta (rhb c93betaa) and cys-->thr at 93beta (rhb c93betat). |
2000-05-18 |
2023-08-12 |
human |
| Y Inai, S Kurashima, T Hirabayashi, K Yokot. Synthesis of delta(E)Phe-containing tripeptide via photoisomerization and its conformation in solution. Biopolymers. vol 53. issue 6. 2000-05-16. PMID:10775064. |
in both peptides, a remarkable noe (approximately 11-13%) was observed for ala c(alpha) h-deltaphe nh pair. |
2000-05-16 |
2023-08-12 |
Not clear |
| B S Zhorov, P D Bregestovsk. Chloride channels of glycine and GABA receptors with blockers: Monte Carlo minimization and structure-activity relationships. Biophysical journal. vol 78. issue 4. 2000-05-15. PMID:10733960. |
the star-like ctb swings necessarily on its way through ring r(6') and its activity inversely correlates with the barrier at r(6'): thr(6')s and ala(2')s in alpha(2) glyr confine the swinging by increasing the barrier, while gly(2')s in alpha(1) glyr and phe(6')s in beta glyr shrink the barrier. |
2000-05-15 |
2023-08-12 |
rat |
| N P Le, H Omote, Y Wada, M K Al-Shawi, R K Nakamoto, M Futa. Escherichia coli ATP synthase alpha subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to the steady state. Biochemistry. vol 39. issue 10. 2000-04-19. PMID:10704230. |
replacement of the conserved alpha subunit arg-376 in the escherichia coli f(1) catalytic site with ala or lys resulted in turnover rates of atp hydrolysis that were 2 x 10(3)-fold lower than that of the wild type. |
2000-04-19 |
2023-08-12 |
Not clear |
| H Czapinska, J Otlewski, S Krzywda, G M Sheldrick, M Jaskólsk. High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence. Journal of molecular biology. vol 295. issue 5. 2000-04-03. PMID:10653700. |
the ala mutations have only an insignificant and localized effect on the binding loop, which retains its wild-type conformation (maximum deviation of loop c(alpha) atoms of 0.7 a at ala13). |
2000-04-03 |
2023-08-12 |
cattle |
| S Rahman, G Flynn, A Aitken, Y Patel, F Hussain, X Lu, J C Loftus, D French, E Wijelath, K Strand, G F Savidg. Differential recognition of snake venom proteins expressing specific Arg-Gly-Asp (RGD) sequence motifs by wild-type and variant integrin alphaIIbbeta3: further evidence for distinct sites of RGD ligand recognition exhibiting negative allostery. The Biochemical journal. vol 345 Pt 3. 2000-03-23. PMID:10642531. |
further evidence for distinct binding sites employing an independent approach was obtained by analysing the binding of the panel of venom proteins to the functionally defective heterodimer alpha(iib)beta(3) ser(123)-->ala expressed on chinese hamster ovary cells. |
2000-03-23 |
2023-08-12 |
Not clear |
| F D Testai, G D Venera, C Pena, M J de Jimenez Bonin. Histidine 186 of the nicotinic acetylcholine receptor alpha subunit requires the presence of the 192-193 disulfide bridge to interact with alpha-bungarotoxin. Neurochemistry international. vol 36. issue 1. 2000-03-08. PMID:10566956. |
this paper studies: (1) the interaction between alpha-bungarotoxin and the peptide alpha173-202--synthesized according to the sequence of the torpedo californica receptor alpha subunit--and between the toxin and the same peptide containing his186 modified with ethoxyformic anhydride or substituted by ala; (2) the influence of the presence of cys192-cys193 disulfide bridge on such interactions. |
2000-03-08 |
2023-08-12 |
Not clear |
| A Scheer, T Costa, F Fanelli, P G De Benedetti, S Mhaouty-Kodja, L Abuin, M Nenniger-Tosato, S Cotecchi. Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha(1b)-adrenergic receptor: effects on receptor isomerization and activation. Molecular pharmacology. vol 57. issue 2. 2000-03-02. PMID:10648631. |
in this study, r143 of the e/dry sequence in the alpha(1b)-ar was mutated into several amino acids (lys, his, glu, asp, ala, asn, and ile). |
2000-03-02 |
2023-08-12 |
Not clear |
| P A Root, A Prince, R E Gunderse. Aggregation of Dictyostelium discoideum is dependent on myristoylation and membrane localization of the G protein alpha-subunit, G alpha 2. Journal of cellular biochemistry. vol 74. issue 2. 1999-08-30. PMID:10404398. |
the putative site for n-terminal myristoylation of g alpha 2 was mutated from gly to ala (g2a) and expressed in the g alpha 2-null cell line, myc2. |
1999-08-30 |
2023-08-12 |
Not clear |
| T Asakura, M Iwadate, M Demura, M P Williamso. Structural analysis of silk with 13C NMR chemical shift contour plots. International journal of biological macromolecules. vol 24. issue 2-3. 1999-08-17. PMID:10342761. |
to determine this relationship, 13c chemical shift contour plots for c alpha and c beta carbons of ala and ser residues, and the c alpha chemical shift plot for gly residues were prepared using atomic co-ordinates from the protein data bank and 13c nmr chemical shift data in aqueous solution reported for 40 proteins. |
1999-08-17 |
2023-08-12 |
Not clear |
| T Asakura, M Iwadate, M Demura, M P Williamso. Structural analysis of silk with 13C NMR chemical shift contour plots. International journal of biological macromolecules. vol 24. issue 2-3. 1999-08-17. PMID:10342761. |
the allowed regions in the 13c chemical shift contour plots for c alpha and c beta carbons of ala and ser residues for the structures in silk fibroins, i.e. |
1999-08-17 |
2023-08-12 |
Not clear |
| T Asakura, M Iwadate, M Demura, M P Williamso. Structural analysis of silk with 13C NMR chemical shift contour plots. International journal of biological macromolecules. vol 24. issue 2-3. 1999-08-17. PMID:10342761. |
there are two area of the phi,psi map which satisfy the observed silk i chemical shift data for both the c alpha and c beta carbons of ala and ser residues in the 13c chemical shift contour plots. |
1999-08-17 |
2023-08-12 |
Not clear |
| A Stea, S J Dubel, T P Snutc. alpha 1B N-type calcium channel isoforms with distinct biophysical properties. Annals of the New York Academy of Sciences. vol 868. 1999-08-12. PMID:10414290. |
two isoforms of the alpha 1b n-type channel from rat brain (alpha 1b-i and alpha 1b-ii) were found to differ in four regions: (1) a glutamate (glu) to glycine (gly) substitution in domain i s3; (2) a gly to glu substitution in the domain i-ii linker; (3) the insertion or deletion of an alanine (ala) in the domain i-ii linker; and (4) the presence or absence of serine/phenylalanine/methionine/glycine (sfmg) in the linker between domain iii s3-s4. |
1999-08-12 |
2023-08-12 |
rat |