ライフサイエンスコーパス: Gly-Gly

1 143 in the "tubulin signature motif" 140Gly-Gly-Gly-Thr-Gly-Ser-Gly146 of Saccharomyces cerevisiae b

2 Gly-Pro-Hyp)(3)-Zaa-Pro-Hyp-(Gly-Pro-Hyp)(4)-Gly-Gly-amide are used to isolate the influence of the r

3 yl-(Gly-Pro-Hyp)3-Gly-Xaa-Yaa-(Gly-Pro-Hyp)4-Gly-Gly-amide.

4 form Ac(Gly-Pro-Hyp)3-Gly-X-Y-(Gly-Pro-Hyp)4-Gly-Gly-NH2 has been designed to evaluate the propensity

5 thin Ac(Gly-Pro-Hyp)3-Gly-X-Y-(Gly-Pro-Hyp)4-Gly-Gly-NH2.

6 yp)3-Gly-psi[(E)CH C]-Pro-Hyp-(Gly-Pro-Hyp)4-Gly-Gly-Tyr-NH2, had a Tm value of 28.3 degrees C.

7 d phage-displayed peptide libraries Ser-[X]4-Gly-Gly-Gly, with Gly and Ser encoded using unique combi

8 d incorporated into a host Ac-(Gly-Pro-Hyp)8-Gly-Gly-Tyr-NH2 peptide to investigate the effect of loc

9 a single polypeptide strand that contains a Gly-Gly sequence approximately midway between the domain

10 er side chains was accomplished via either a Gly-Gly spacer (PHPMA-GG-I) or with no spacer between I

11 Strikingly, substitution of one of a Gly-Gly pair with highly charged residues that significa

12 f a short stretch of hydrophobic residues, a Gly-Gly pair, a CX(6)CC motif, and a bulky hydrophobic r

13 When a Gly-Gly-His tripeptide is placed on either the Watson-Cr

14 5 and substituted the 11-residue loop with a Gly-Gly dipeptide that bridges the deletion without intr

15 A methods by linking two IL5 monomers with a Gly-Gly linker.

16 wild-type two-residue loop (Asp-Ala) with a (Gly-Gly) linker accelerates both unfolding and refolding

17 tide was modified to Gly-Pro-Arg-Pro-Pro-Aba-Gly-Gly-(D)-Ala-Gly to permit efficient binding of 99mTc

18 e the cyclic model peptide cyclo(Cys-Thr-Abu-Gly-Gly-Ala-Arg-Pro-Asp-Phe): (i). side-chain anchoring

19 The achiral -Gly-Gly- linker permits helix termination as a Schellman

20 la-Gly-Ala, Ala-Ala-Gly and Gly-Gly-Gly-Ala, Gly-Gly-Ala-Gly).

21 An endogenous Tc chelation site (Ala-Gly-Gly-Cys-Gly-His) was added to the N-terminus of anne

22 able 500-fold increase in affinity for AMPhe-Gly-Gly, which bound to Q7 with an equilibrium dissociat

23 ., Gly-Ala-Ala, Ala-Gly-Ala, Ala-Ala-Gly and Gly-Gly-Gly-Ala, Gly-Gly-Ala-Gly).

24 d were of sequence X-Gly-Gly, Gly-X-Gly, and Gly-Gly-X (X = Trp, Phe, Tyr, and His).

25 the model compounds Tyr-Gly-Gly-Phe-Leu and Gly-Gly-Trp-Gly indicated that tyrosine transferred appr

26 e methylene groups of the parent linker) and Gly-Gly were synthesized.

27 the synthetic substrates Lys-Pro-Gln-pNA and Gly-Gly-Gln-pNA, the overall K(m) values were determined

28 in Npl3 purified from yeast: whereas 10 Arg-Gly-Gly (RGG) tripeptides were exclusively dimethylated,

29 ding domains (RBDs also called RRMs) and Arg-Gly-Gly (RGG) motifs.

30 er recognition site (Gly-Gly-Ile-Glu-Gly-Arg-Gly-Gly) for the protease factor Xa, also containing a t

31 recognition sequence of Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe, with the COOH-terminal flanking glycine

32 catalyzed hydrolysis of Ub-AMC and Z-Leu-Arg-Gly-Gly-AMC.

33 zyme with the fluorogenic substrate (Leu-Arg-Gly-Gly-NH)2-rhodamine.

34 id sequence motif contains multiple RGG (Arg-Gly-Gly) boxes characteristic of RNA-binding proteins.

35 r RNA binding domains and the C-terminal Arg-Gly-Gly repeats.

36 The Arg-Gly-Gly repeats within the low-complexity region are req

37 hat activate hydrolysis of benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin are 50-100 fold low

38 -catalyzed transamidation of gammaGlu-AMC by Gly-Gly to form gammaGlu-Gly-Gly.

39 ions of the lymph node cells had a conserved Gly-Gly motif.

40 Trp replacements for conserved Gly-Gly pairs between the N- and C-terminal six-helix bu

41 Because sentrin possesses the conserved Gly-Gly residues near the C terminus, it is likely that

42 When the conserved Gly-Gly residues of sentrin were changed to Gly-Ala, onl

43 ended segment that contains a well-conserved Gly-Gly motif.

44 gest that the amino acid sequence containing Gly-Gly that is located at the C terminus of the D1-D2 l

45 triple-helical peptides containing different Gly-Gly-Y guest triplets, confirm the destabilizing effe

46 conserved internal ubiquitin-like diglycine (Gly-Gly) motif.

47 N-unsubstituted alpha-amino acids, dipeptide Gly-Gly, and also benzylamine were used as the amine com

48 water molecule on six protonated dipeptides (Gly-Gly+H(+), Gly-Ala+H(+), Ala-Gly+H(+), Ala-Ala+H(+),

49 irulence peptide 1 (vp1), a highly expressed Gly-Gly peptide-encoding gene in chinchilla middle ear e

50 idues 9-35) of rabbit I-BABP with a flexible Gly-Gly-Ser-Gly linker results in the loss of stabilizin

51 ion of the two central residues, except for -Gly-Gly-, the most stable beta-turn type is always found

52 ed twist of beta-strands, type I' turns for -Gly-Gly- are found to occur with high frequency, even wh

53 of gammaGlu-AMC by Gly-Gly to form gammaGlu-Gly-Gly.

54 ]-CONH(2); X = GGNle, GENle, or NleGE; GG = -Gly-Gly- and GE = -Gly-Glu-} peptides.

55 acid O-linked glycopeptide (pGlu-Ser-Glu-Glu-Gly-Gly-Ser-Asn-Ala-Thr-Lys-Lys-Pro-Tyr-Ile-Leu-OH, pGlu

56 ly-Gly and Gly-Leu-Leu-Gly, Gly-Leu-Gly-Gly, Gly-Gly-Ala-Gly) but also peptides with the same amino a

57 Among the small peptides 2-31, (H)Gly-Gly-Phe-Leu(OMe) (30) reduced prostaglandin producti

58 The peptide hydrates Gly-Gly-Val x 2H(2)O (GGV) and Gly-Ala-Leu x 3H(2)O (GAL

59 eptide BH17, Boc-Val-Ala-Leu-Aib-Val-Ala-Leu-Gly-Gly-Leu-Phe-Val-DPro-Gly-Leu- Phe-Val-OMe (where Boc

60 eu, Leu-Gly-Gly and Gly-Leu-Leu-Gly, Gly-Leu-Gly-Gly, Gly-Gly-Ala-Gly) but also peptides with the sam

61 uctures (e.g., Gly-Ala-Ala, Gly-Ala-Leu, Leu-Gly-Gly and Gly-Leu-Leu-Gly, Gly-Leu-Gly-Gly, Gly-Gly-Al

62 e optimized in the tetrapeptide fixed ligand Gly-Gly-Ala-Gly, as shown by data for 15 fixed ligands.

63 et-Ala-Ala-Arg-Ala), His-peptide (Ac-Val-Lys-Gly-Gly-His-Ala-Lys-Tyr-Gly-Gly-Met(OX)-Ala-Ala-Arg-Ala)

64 d to sulfone, and HisMet-peptide (Ac-Val-Lys-Gly-Gly-His-Ala-Lys-Tyr-Gly-Gly-Met-Ala-Ala-Arg-Ala).

65 velopment of antibodies recognizing the Lys--Gly-Gly (diGly) remnant from ubiquitinated proteins foll

66 at a time, by a peptide linker consisting of Gly-Gly-Ser- repeat sequences, which are believed to hav

67 mma-boroGlu is an uncompetitive inhibitor of Gly-Gly-promoted transamidation of gammaGlu-AMC.

68 replaced in turn by structureless linkers of Gly-Gly-Ser repeat sequences, and the effect on the prot

69 We established that the presence of Gly-Gly at the P1'-P2' positions is optimal for cleavage

70 The presence of Gly-Gly-Y triplets may play an important role in specifi

71 : (i) molecular dynamics (MD) simulations of Gly-Gly-X-Gly-Gly pentapeptides in water at 298 K with e

72 y-Trp-Gly, and with 40-fold specificity over Gly-Gly-Trp.

73 ng the original termini with a three-peptide Gly-Gly-Gly linker, and conferring new termini to four d

74 conformation of the model tripeptide Ac-Phe-Gly-Gly-NH-CH(3) as starting structures.

75 binds and dimerizes Trp-Gly-Gly (1) and Phe-Gly-Gly (4) with high affinity (ternary K = 10(9)-10(11)

76 formations from the Protein Data Bank of Phe-Gly-Gly protein fragments containing Ar-HN interactions.

77 hylase-preferred recognition sequence of Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe, with the COOH-terminal

78 e dominant repeat of this protein is Gly-Pro-Gly-Gly-X, which can appear up to 63 times in tandem arr

79 e NH2-terminal sequence, NH2-Phe-Val-Pro-Pro-Gly-Gly, starting with residue 41 of the intact Rieske p

80 or were not hydrolyzed (an exception was Pro-Gly-Gly, which cleaved at a moderate rate).

81 ther two motifs in the flagelliform protein, Gly-Gly-X and a spacer that disrupts the glycine-rich re

82 tive site lead to a juxtaposition of the Prx Gly-Gly-Leu-Gly and Srx ATP-binding motifs, providing a

83 tic loop, immediately preceding the sequence Gly-Gly-Gly-Ala-Asn.

84 t 20 N-terminal amino acid residues (Val-Ser-Gly-Gly-Glu-Ala-Asn-Thr-Leu-Pro-His-Val-Ala-Phe-Tyr-Ile-

85 a flexible peptide linker containing several Gly-Gly-Ser repeats.

86 a-helical motif (residues 9-35) with a short Gly-Gly-Ser-Gly linker dramatically affects the protein

87 A diglycine linker recognition site (Gly-Gly-Ile-Glu-Gly-Arg-Gly-Gly) for the protease factor

88 resulted in no change in affinity for tBuPhe-Gly-Gly, but a remarkable 500-fold increase in affinity

89 n which the residue preceding the C-terminal Gly-Gly (diGly) is replaced with a lysine (SUMO(KGG)).

90 ne branched peptides in which the C-terminal Gly-Gly fragment of ubiquitin is attached to the epsilon

91 Furthermore, the conserved C-terminal Gly-Gly residues are required for sentrinization to occu

92 d peptides in which the ubiquitin C-terminal Gly-Gly residues are retained on the modified lysine res

93 ired the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.

94 fold including a conserved carboxy-terminal Gly-Gly motif.

95 The results indicate that Gly-Gly-Y triplets, which are adjacent to the epitope, h

96 The Gly-Gly modification is stable and both tandem mass spec

97 The Gly-Gly-Gly-Ala-Asn-X-X-X-X-Gly-Tyr motif of loop C and

98 on in stabilizing the conformation about the Gly-Gly turn, resulting in a specific orientation of the

99 pe II or II' beta-turn conformation, but the Gly-Gly unit in the compound derived from 4-benzyl-Aca d

100 r aerobic, but not anaerobic, conditions the Gly-Gly-Gly chromophore sequence cyclizes and incorporat

101 lysis of TCR affinity/avidity correlated the Gly-Gly motif with lower affinity and retention of the T

102 a are consistent with this as a role for the Gly-Gly sequence between the regulatory and substrate bi

103 The results illustrate the importance of the Gly-Gly sequence at positions 36 and 37 and the 37 HN-35

104 This analysis revealed that the Gly-Gly motif formed by Gly-65 and Gly-66 and the beta-s

105 A previous study determined that the Gly-Gly sequence at the junction between the regulatory

106 he present study shows that mutations to the Gly-Gly sequence at the junction of the substrate and nu

107 The former can be ascribed to the Gly-Gly-Ala motif while the latter is assigned to the po

108 The -Gly-Gly- and -Ala-Ala- mutants exhibit intermediate E(ox

109 dues of the turn (Gly57 and Asp58) with the -Gly-Gly-, -Gly-Ala-, -Ala-Gly-, and -Ala-Ala- dipeptidyl

110 s, which introduce bulky residues into tight Gly-Gly interdomain interactions on the periplasmic side

111 a 20-beta 21 hairpin (residues 422 to 436 to Gly-Gly) improved overall protein expression.

112 We find that Q8.MV binds Trp-Gly-Gly with high affinity (K(a) = 1.3 x 10(5) M(-1)), w

113 Q8 selectively binds and dimerizes Trp-Gly-Gly (1) and Phe-Gly-Gly (4) with high affinity (tern

114 1.1.1.95) from Escherichia coli contains two Gly-Gly sequences that have been shown previously to hav

115 drogenase from Escherichia coli contains two Gly-Gly sequences that occur at junctions between domain

116 ediamine)) and 0.24 x 10(4) M-1 s-1 (Abz-Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-Gly-Arg-Pro-Glu-EDDnp), with

117 urotransmitter methionine enkephalin (Ac-Tyr-Gly-Gly-Phe-Met) and synthetic peptides termed Met-pepti

118 M-1 s-1 (Abz-Val-Pro-Arg-Met-Glu-Lys-Arg-Tyr-Gly-Gly-Phe-Met-Gln-EDDnp+ ++; where Abz is ortho-aminob

119 injection testing of the model compounds Tyr-Gly-Gly-Phe-Leu and Gly-Gly-Trp-Gly indicated that tyros

120 e endogenous opioids leucine enkephalin (Tyr-Gly-Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly-

121 -Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly-Phe-Met).

122 -peptide (Ac-Val-Lys-Gly-Gly-His-Ala-Lys-Tyr-Gly-Gly-Met(OX)-Ala-Ala-Arg-Ala), in which a Met is oxid

123 peptides termed Met-peptide (Ac-Ala-Lys-Tyr-Gly-Gly-Met-Ala-Ala-Arg-Ala), His-peptide (Ac-Val-Lys-Gl

124 -peptide (Ac-Val-Lys-Gly-Gly-His-Ala-Lys-Tyr-Gly-Gly-Met-Ala-Ala-Arg-Ala).

125 n well conserved ancestral opioid motif (Tyr-Gly-Gly-Phe).

126 eptide subunits in Leu-enkephalin (H(2)N-Tyr-Gly-Gly-Phe-Leu-OH), which is believed to bind to opiod

127 which recognizes the pan-opioid sequence Tyr-Gly-Gly-Phe at the N terminus of most endogenous opioid

128 by the lack of effect of the tripeptides Tyr-Gly-Gly and Gly-Ala-Gly on the activity of PKC.

129 otease contains a characteristic Arg-Val-Val-Gly-Gly motif that may serve as a proteolytic activation

130 antibodies that recognize the Lys-varepsilon-Gly-Gly (K-varepsilon-GG) remnant produced by trypsin di

131 nking the two hIL5 chain coding regions with Gly-Gly linker.

132 sed direct DNA cleavage relative to Ni(II) x Gly-Gly-His was observed when (1) the amino-terminal pep

133 was slightly increased relative to Ni(II) x Gly-Gly-His, however, not to an extent necessary to acco

134 ns of the above systems, along with Ni(II) x Gly-Gly-His, indicated that the stereochemistry of the a

135 DNA cleavage by diastereoisomers of Ni(II) x Gly-Gly-His-derived metallopeptides was investigated thr

136 A an order of magnitude better than Ni(II) x Gly-Gly-His.

137 eading to an interaction similar to Ni(II) x Gly-Gly-His.

138 cular dynamics (MD) simulations of Gly-Gly-X-Gly-Gly pentapeptides in water at 298 K with exhaustive

139 nd cleave at a position following a p4-Leu-X-Gly-Gly-p1 tetrapeptide, but it is unknown whether these

140 The peptides studied were of sequence X-Gly-Gly, Gly-X-Gly, and Gly-Gly-X (X = Trp, Phe, Tyr, an

141 es at the N-terminus of model tripeptides (X-Gly-Gly), resulted in no change in affinity for tBuPhe-G

142 hydrolyzes rapidly the fluorogenic peptide Z-Gly-Gly-Leu-AMC and very slowly certain other chymotryps

143 % MS SI restoration for the Z-Gly-Gly-Val and bradykinin peptides were 75-83% while %