ライフサイエンスコーパス: Phe residue

1 no acid residues (one Trp, eight Tyr, and 13 Phe residues).

2 n the aromatic ring stack with the conserved Phe residue.

3 n ionization being protected by Leu, Tyr and Phe residues.

4 e results indicate a catalytic role of these Phe residues.

5 , possibly due to quenching with neighboring Phe residues.

6 ation of the Tyr residue and approximately 4 Phe residues.

7 ariant lacking the N-terminal phenylalanine (Phe) residue.

8 highly conserved hydrophobic element Val-Ile-Phe (residues 11-13) and the adjacent positively charged

9 Mutation of Tyr-196 in glycogenin-2 to a Phe residue abolished the ability of glycogenin-2 to sel

10 shows that binding occurs at the N-terminal Phe residue and that the N-terminus unfolds to enable bi

11 n on graphene due to an even distribution of Phe residues and hydrophilic residues.

12 shift perturbation mapping of (15)N-labeled Phe residues and x-ray crystallography to examine the li

13 GD', redox-sensitive Cys and hydrophobic Trp/Phe residues argues for their functional relevance and c

14 , and the Thr residue at position 24 and the Phe residue at position 25 are individually indispensabl

15 were highly functional substitutions for the Phe residue at position 45.

16 ies previously identified a highly conserved Phe residue at the N-terminus of Thermus aquaticus MutS

17 Phe residues at aa 3 and 9 are critical for an N-termina

18 clic decapeptide antibiotic tyrocidine has D-Phe residues at positions 1 and 4, produced during pepti

19 Taken together, these results indicate that Phe residues at positions 3 and 9 have been selected for

20 Phe-Phe interaction between highly conserved Phe residues at the -4 position in EF-hand III (F[-4]; T

21 A cluster of Phe residues at the fulcrum of this pivot point allows f

22 In contrast, the substitution of 10 Phe residues at the N terminus of v-Rel does not enable

23 nalysis highlighted highly conserved Ile and Phe residues at the RfaH interdomain interface.

24 ggest gating was associated with shifts of a Phe residue between open and closed conformations plus a

25 produced during peptide chain growth from L-Phe residues by 50 kDa epimerase (E) domains embedded, r

26 all and highly hydrophobic with a cluster of Phe residues composing the active site roof.

27 of sanguinamide B showed that only l- and d-Phe residues controlled the macrocycle conformation.

28 taining an Ala substitution for the critical Phe residue did not compete for the interaction at all.

29 There are seven Phe residues, distributed throughout the protein; they p

30 The remaining two Phe residues do not have homologs in isoprene synthases

31 s nonessential Trp residues were replaced by Phe residues, eliminating intrinsic fluorescence.

32 ral and weakly basic capping groups of the D-Phe residue exhibited excellent MC4R selectivity against

33 inding was dependent upon a highly conserved Phe residue (F65) that in human POT1 directly contacts t

34 Mutations of the central Phe residue favored the closed KAT1 channel, whereas mut

35 stently, a GSK mutant with substitution of a Phe residue for residue Tyr-216, which showed one-fifth

36 One of these residues is homologous to a Phe residue found in the active site of isoprene synthas

37 The presence of a polar Asn212 in place of a Phe residue found in the cognate position of other mu cl

38 The Phe residue immediately preceding the first Ca(2+) ligan

39 as no obvious preference toward the aromatic Phe residue in comparison to the hydrophobic Leu or Ile

40 The data reveal an unusual role for the Phe residue in that it promotes the unbending, not bendi

41 with the major capsid protein; and (iii) the Phe residue in the CMV minimal interaction domain is cri

42 The structural analysis revealed that the Phe residue in the F(X)(6)LL motif is buried in the tran

43 ese single-point mutations in HTB1 replace a Phe residue in the hydrophobic core with either a Glu or

44 The hydrophobic Phe residue in the P2 position of the RSL region is cons

45 own that substitution of Ala for one or more Phe residues in calmodulin (CaM) imparts a temperature-s

46 Phe residues in Delta-somatostatin are hypothesised as i

47 port for a catalytic role of these and other Phe residues in providing anion-aromatic interactions th

48 The locations of these four critical Phe residues in relation to other essential and/or hydro

49 equence is used to replace the hAGRP Arg-Phe-Phe residues in the "mini"-AGRP (hAGRP87-120, C105A) tem

50 Inserting Phe residues in the cavity around the myristoyl group in

51 an Lys residues, and the inclusion of Tyr or Phe residues in the hinge regions between anchoring doma

52 de and SWNTs is examined by substituting the Phe residues in the nano-1 sequence with tyrosine and p-

53 Altering the C-terminal-most Pro or Phe residues in the SSB-Ct strongly impairs SSB-Ct bindi

54 d the polarity and steric bulk of one of the Phe residues in the supercore of the hexamer.

55 that contain a pentafluorophenylalanine (F(5)Phe) residue in the hydrophobic core.

56 Finally, we show that there is an ideal Phe residue (in this case L-Phe) for generating compound

57 Moreover, introduction of these Phe residues into the dityrosine motif of the RON kinase

58 Mutation analysis revealed that the Phe residue is absolutely critical for the binding, sinc

59 These data suggest that the Phe residue is probably involved in folding of alpha(2B)

60 r variant (Phe-14(M)) in which a single core Phe residue is substituted with Met.

61 r9 in 1 sequence with the Btz or the (3,4-Cl)Phe residues led to superagonists 6 (UPG-100) and 10 (UP

62 These conserved Phe residues may have a role in the conversion of high m

63 ar Tyr residue 759 of gp130 is replaced by a Phe residue, mediates prolonged signaling and is not cro

64 Acylation of the NH2 group of the 4F-D-Phe residue of 3-propyl analog 23 significantly increase

65 Carbon-13 labeling of the Phe residue of penetratin was used to shift the intense

66 ing steric drug interaction with the primary Phe residue of the binding site.

67 region at the N-terminal side of the central Phe residue of the CMV interaction domain played a role

68 action between the hydrophobic Leu, Pro, and Phe residues of TBP with the TA, AT, AA, TT, and CG step

69 e hydrophobic residues are centered around a Phe residue on one side of the alpha-helix.

70 4F (Ac-DWFKAFYDKVAEKFKEAF-NH(2)), with four Phe residues on the nonpolar face of the amphipathic alp

71 hilic alpha-helix wherein the phenylalanine (Phe) residues on the hydrophobic face of the helix inter

72 d at backbone carbonyl sites of Tyr, Leu, or Phe residues or at side-chain methyl sites of Ala residu

73 a "Phe clamp," a heptad of narrowly apposed Phe residues (Phe-427), that catalyzes the unfolding and

74 henylalanines and tyrosines, including three Phe residues (Phe-61, Phe-312, and Phe-526) forming an a

75 in the monomer of the b 6 f complex, and (b) Phe residues (Phe133/Phe135) of subunit IV are important

76 CKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED det

77 calized to the first cytoplasmic domain at a Phe residue (position 400), which is conserved in all ni

78 r residue predicts dipeptide ligase while an Phe residue predicts both depsipeptide and dipeptide lig

79 the nonpolar face (Leu(3) and Leu(14)) with Phe residues produced the peptide 4F (so named because o

80 nd that the Arg(481) and the Asp-Leu-Pro-Glu-Phe residues (residues 488-492) were critical for alpha(

81 The two Phe residues straddle the adenine ring of bound APS.

82 n unusual twin-His site in the middle, and a Phe residue that blocks the channel for small-molecule t

83 thases but occupy the same space as a second Phe residue that closes off the isoprene synthase active

84 A Phe residue that shutters the water-filled central apert

85 on of actin tails, conservatively changed to Phe residues; the other had the A36R open reading frame

86 s of the VSD, when hydrated around a central Phe residue, to the closed state of the channel.

87 We have tested the role of the Phe residues using site-directed mutagenesis, double-mut

88 ions revealed that the two membrane-proximal Phe residues were critical for the proper UL20p membrane

89 e point where binding was abolished when all Phe residues were modified to Ala.

90 Active site Phe residues were most affected by the binding of azole

91 himeric ligands, the antagonist AGRP Arg-Phe-Phe residues were replaced by the melanocortin agonist H

92 effective substitutes for each of the three Phe residues, whereas replacement with smaller or polar

93 Replacement of the D-Phe residue with conformationally biased beta-methyl der

94 The replacement of the aromatic Phe residue with Leu has no discernible effect on the vi

95 Modeling based on NMR data indicates the Phe residue within a GF interruption is located on the o

96 This work revealed that Phe residues within the UL20p carboxyl terminus are invo

97 on either side of a conserved phenylalanine (Phe) residue within the S2 and S3 alpha-helices of the v

98 esidue at the -4th position of EF III to the Phe residue (Y81F), to bring in the Phe-Phe interaction