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 proRaxX is cleaved at a Gly-Gly motif, yielding a mature peptide that retains th

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

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

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

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

14 he structure of one such antibody bound to a Gly-Gly-Met peptide to reveal the molecular basis for it

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

16 acement of two beta-hairpin sequences with a Gly-Gly and shorteing of a beta-hairpin resulted in a pr

17 5 and substituted the 11-residue loop with a Gly-Gly dipeptide that bridges the deletion without intr

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

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

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

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

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

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

24 with (68)Ga-NOTA-GZP (where GZP is beta-Ala-Gly-Gly-Ile-Glu-Phe-Asp-CHO) to detect early intestinal

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

26 L-proline, L-serine, L-histidine, D-alanine, Gly-Gly, and Gly-Gly-Gly, to achieve astrocyte-specific

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

28 ., Gly-Ala-Ala, Ala-Gly-Ala, Ala-Ala-Gly and Gly-Gly-Gly-Ala, Gly-Gly-Ala-Gly).

29 serine, L-histidine, D-alanine, Gly-Gly, and Gly-Gly-Gly, to achieve astrocyte-specific delivery of n

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

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

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

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

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

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

36 r protein that binds RNA through RRM and Arg-Gly-Gly (RGG) motifs.

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

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

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

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

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

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

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

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

45 We compared (68)Ga-NOTA-GZP (betaAla-Gly-Gly-Ile-Glu-Phe-Asp-CHO) PET images with those obtai

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

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

48 These RFs possess a conserved Gly-Gly-Gln (GGQ) peptide release motif, of which the Q

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

82 ained for the complex of Q8 with the peptide Gly-Gly-Leu-Tyr-Gly-Gly-Gly (GGLYGGG) and reveals struct

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

100 CRL2 substrate receptor targeting C-terminal Gly-Gly degrons, is regulated through interconversion be

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

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

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

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

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

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

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

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

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

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

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

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

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

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

115 water which combines the selectivity of the Gly-Gly-His (GGH) peptide probe with the sensitivity of

116 e dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enabl

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

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

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

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

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

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

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

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

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

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

127 omodimers FemA and FemB sequentially add two Gly-Gly dipeptides.

128 1.1.1.95) from Escherichia coli contains two Gly-Gly sequences that have been shown previously to hav

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

130 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

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

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

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

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

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

136 mplex of Q8 with the peptide Gly-Gly-Leu-Tyr-Gly-Gly-Gly (GGLYGGG) and reveals structural details of

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

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

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

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

141 oid peptides share the amino acid motif, Tyr-Gly-Gly-Phe-, at the N-terminus.

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

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

144 peptide fragments containing the shared Tyr-Gly-Gly-Phe- motif.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

160 % MS SI restoration for the Z-Gly-Gly-Val and bradykinin peptides were 75-83% while %