ライフサイエンスコーパス: Ile residue

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1 ach containing either an allo-Thr or an allo-Ile residue.

2 idue in comparison to the hydrophobic Leu or Ile residues.

3 ments for the methyl groups of Val, Leu, and Ile residues.

4 e-chain stereochemistry of individual Thr or Ile residues.

5 n intersubunit salt link, and several buried Ile residues.

6 of a salt bridge between the new N-terminal Ile (residue 16) and Asp194.

7 These results indicate that the Arg and/or Ile residues adjacent to the C-terminus are necessary (b

8 Lys-1374 (human numbering) in RBF to Arg or Ile residues almost completely abolishes signal transduc

9 esidue in peptides containing up to five Leu/Ile residues and molecular masses up to 3000 Da.

10 The sensitive enzyme has an Ile residue, and the resistant one has a Leu residue at

11 It is noteworthy that the Val and Ile residues are highly conserved among the GPCRs carryi

12 es were obtained by the incorporation of the Ile residue at the P5 and P6 positions.

13 tide showed that the phosphotyrosine and the Ile residue at the pY + 3 position are recognized by the

14 This arrangement allows two conserved Leu/Ile residues at Asp(+1) and Asp(+4) to be presented on t

15 ization signal to the HA1 N-terminal Ile-Cys-Ile residues at positions 3 to 5.

16 obic character; (3) ISDs tend to have Leu or Ile residues at their core; (4) ISDs are approximately e

17 ell by lactam formation between Pro and N-Me-Ile residues, but attempted lactonizations of the Pro ca

18 cid sequences, including identity of Leu and Ile residues, can be accurately obtained solely by means

19 the full-length Vpr also helped identify Leu/Ile residues critical for Vpr interaction with the cellu

20 th carboxypeptidase Y, which cleaved Tyr and Ile residues from the carboxyl terminus of the alpha sub

21 elines we unambiguously identified every Leu/Ile residue in peptides containing up to five Leu/Ile re

22 the phi, psi backbone dihedral angles of the Ile residue in the eighth position is necessary and suff

23 nstrated, for the first time, that every Leu/Ile residue in the variable regions of a monoclonal anti

24 The results show that beta-stranded Leu and Ile residues in all LRRs are important but not equally.

25 In this work, the beta-stranded Leu/Ile residues in all LRRs of the human LHR and FSHR were

26 s spectrometer, to reliably identify Leu and Ile residues in proteins and peptides.

27 We converted the three Ile residues in Sup35NM to Leu and then replaced 16 sing

28 ched Ile, include strong, sharp signals from Ile residues in the globular C-terminal domain (CTD) wit

29 Point mutational analysis of the Leu/Ile residues in the LR domain suggested that multiple Le

30 he binding site align with essential Leu and Ile residues in the RII-selective tethering domain of pr

31 Positioning of incorrect Leu/Ile residues in variable domains, especially in CDRs (co

32 indicate that replacing Thr with the larger Ile residue leads to greater burial of residue 105 and h

33 ments were successful in all 22 cases of Leu/Ile residues, leaving no doubts in identification.

34 the full-length Vpr also helped identify Leu/Ile residues may be involved in maintaining the leucine-

35 in the LR domain suggested that multiple Leu/Ile residues may be involved in maintaining the leucine-

36 no acid analogues of the (1) Glu-Glu and (2) Ile residues of the Lck SH2 domain peptide ligand Ac-pTy

37 e chain stereochemistry of individual Thr or Ile residues on the properties of the ShK protein.

38 complex with ligands containing P(0) Leu or Ile residues reveals two distinct modes of accommodation

39 Correlating with a Val-to-Ile residue substitution in the bsNOS heme pocket, the F

40 -relaxation data for the delta1 positions of Ile residues that are distributed over the 3D-fold of P2

41 cted mutageneses, the latter directed to two Ile residues that play an important role in DNA recognit

42 We find that mutation of the corresponding Ile residue to Tyr in Drosophila beta4GalNAc-T1 converts

43 Asp carboxylate, resulting in movement of an Ile residue toward the heme.

44 ids and the number of targeted isomeric (Leu/Ile) residues varied between 1 and 7.

45 )C,(15)N]epsilon186 containing Val, Leu, and Ile residues with protonated methyl groups, which allowe

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