ライフサイエンスコーパス: peptide backbone

1 ith the helical amide carbonyl groups of the peptide backbone.

2 of the N and C termini to form a continuous peptide backbone.

3 ) the side chain ammonium group, and (3) the peptide backbone.

4 beta radical which is poised to fragment the peptide backbone.

5 not exert major conformational effect on the peptide backbone.

6 3, which forms three hydrogen bonds with the peptide backbone.

7 progressively poorer solvent quality for the peptide backbone.

8 f the solvent alters solvent quality for the peptide backbone.

9 encies of the osmolytes to interact with the peptide backbone.

10 oduce sequence information across the entire peptide backbone.

11 between adjacent carbonyl carbons along the peptide backbone.

12 f intramolecular H-bonds present in the beta-peptide backbone.

13 agmentation by ETD occurs randomly along the peptide backbone.

14 large favorable interaction of urea with the peptide backbone.

15 onding with the N-H of Gly216 (2.9 A) in the peptide backbone.

16 , and so on) at specific locations along the peptide backbone.

17 which also contribute to the rigidity of the peptide backbone.

18 unpaired electron at an alpha-C atom of the peptide backbone.

19 n and the formation of hydrogen bonds to the peptide backbone.

20 d to disrupt conserved hydrogen bonds to the peptide backbone.

21 genetically conserved hydrogen bonds to the peptide backbone.

22 is at any one of several positions along the peptide backbone.

23 ight into the conformational dynamics of the peptide backbone.

24 rgely by direct interaction of urea with the peptide backbone.

25 Hyp and also between polysaccharides and the peptide backbone.

26 ducing site-specific isotope-labels into the peptide backbone.

27 waters, and the carbonyls and amides of the peptide backbone.

28 ical and unique conformational effect on the peptide backbone.

29 dicals located on the (alpha)C moiety of the peptide backbone.

30 t decreases the solvent accessibility of the peptide backbone.

31 tains thiazole and oxazole heterocycles in a peptide backbone.

32 tural changes in amino acid residues and the peptide backbone.

33 om transfer from the Calpha positions of the peptide backbone.

34 the insertion of OM moieties as part of the peptide backbone.

35 0 amino acids along dynein's one-dimensional peptide backbone.

36 er between the carbohydrate (GalNAc) and the peptide backbone.

37 titutions provide evidence for a kink in the peptide backbone.

38 s bound parallel to the alpha-helices of the peptide backbone.

39 er binding mode leads to the cleavage of the peptide backbone.

40 h side-chain-induced axial retraction of the peptide backbone.

41 pectroscopy was used to probe changes in the peptide backbone.

42 he bond rotational degrees of freedom in the peptide backbone.

43 leavage with concurrent fragmentation of the peptide backbone.

44 helices and covalent interactions along the peptide backbone.

45 e via a network of multiple H-bonds with the peptide backbone.

46 ided direct evidence of cleavages within the peptide backbone.

47 g evidence for distinct conformations of the peptide backbone.

48 ng otherwise impossible conformations in the peptide backbone.

49 and the location of the modification on the peptide backbone.

50 O-glycans and a database search strategy for peptide backbones.

51 ble interaction between the osmolyte and the peptide backbone, a solvophobic thermodynamic force that

52 eferential fragmentation of cross-links over peptide backbones, a desired feature for MS(n) analysis.

53 oligopeptides and duplexes indicate that the peptide backbone acts as a scaffold for the directed ass

54 How changes in the structure of the peptide backbone affect the loading of peptides onto MHC

55 patial distance of the pyridyl moiety to the peptide backbone affects the metal coordination.

56 n trap (QLT) and induce fragmentation of the peptide backbone along pathways that are analogous to th

57 hat catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimic

58 ave the disulfide bond more readily than the peptide backbone amide bonds that enabled the identifica

59 of proteins catalyzes the phosphorylation of peptide backbone amide bonds, which leads to the formati

60 ution of the protonation of nitrogens in the peptide backbone amide bonds.

61 s revealed that ion conductance tallies with peptide backbone amide I vibrational changes at 1,665(-)

62 s corresponding to cleavages at all possible peptide backbone amine bonds, except on the N-terminal s

63 different groups in proteins, including the peptide backbone, amino acid side chains, internal water

64 s an exocyclic amide positioned alpha to the peptide backbone, an arrangement that is not found among

65 f this photoproduct requires cleavage of the peptide backbone and a dramatic reorganization of trypto

66 is the incorporation of aspartic acid in the peptide backbone and acid sensitive O-sulfated glycan ch

67 onformational change is propagated along the peptide backbone and affects the position of a tryptopha

68 ive to each other based on continuity of the peptide backbone and by imposing a distance restraint re

69 Cyclic peptide backbone and cystine constraints were used to de

70 his study, we explore the role of the cyclic peptide backbone and cystine ladder in the structure, st

71 They involve changes in the peptide backbone and in the H-bond of the side chain of

72 anges into individual contributions from the peptide backbone and residue side chains.

73 limit the conformational flexibility of the peptide backbone and retain the relative orientation of

74 istances in the complex, which constrain the peptide backbone and side chain conformations in the GPG

75 We demonstrate constraint of peptide backbone and side-chain conformation with 3D (1)

76 in reality, side chains are attached to the peptide backbone and surrounded by other side chains in

77 the few replacements that locally orient the peptide backbone and the amino acid side chain in a pred

78 Spectral contributions from the peptide backbone and the amino acid side chains were cal

79 ic choice depends on the conformation of the peptide backbone and the configuration and conformation

80 her complicated by fragmentation of both the peptide backbone and the glycan moiety.

81 ent exposed acidic pocket formed between the peptide backbone and the HLA-DP2 beta-chain alpha-helix

82 Twelve conserved hydrogen bonds between the peptide backbone and the MHC are a prominent sequence-in

83 ic cystine ladder motif, comprising a cyclic peptide backbone and three parallel disulfide bonds, is

84 Given the importance of the peptide backbone and Trp side chains for ion permeation,

85 repeat constrained by a head-to-tail cyclic peptide backbone and two cross-bracing disulfides.

86 amino acids are constrained by an end-to-end peptide backbone and two or three disulfide bonds to cro

87 endent on the precise stereochemistry of the peptide backbone and was blocked with a soluble TCR.

88 edicted gradient of hydrophobicity along the peptide backbone and with net positive charge; they corr

89 her NCE values preferentially fragmented the peptide backbone and, thus, provided information needed

90 optimal conditions for the fragmentation of peptide backbones and glycoconjugates.

91 lding block due to its rigidifying effect on peptide backbones and its electrophilicity which allows

92 ids and non-peptidic constraints that modify peptide backbones and side chains to fine-tune cyclic pe

93 wo-, three-, or four-atom distances from the peptide backbone, and each ensures that attached sugars

94 n indole anchors relative to the lipids, the peptide backbone, and the membrane/water interface.

95 their N-linked glycan composition, while the peptide backbone appears to be conserved.

96 e thioester substrates in which parts of the peptide backbone are altered either by the replacement o

97 substrate, revealing that some parts of the peptide backbone are important for cyclization, while ot

98 Hydrogen bonds to the peptide backbone are loosened rapidly compared with the

99 Thioamide modifications of the peptide backbone are used to perturb secondary structure

100 ubstitution increases the flexibility of the peptide backbone around the site of mutation.

101 hanges in the mobilities and dynamics of the peptide backbone as a result of antibody binding.

102 f local solvation as folding progresses, the peptide backbone as modeled by alanine oligomers shifts

103 ous transition metal ions bound close to the peptide backbone as the acceptor.

104 as histidine, aspartate, glutamate, and the peptide backbone as well.

105 ed in pSer13 Noxa, indicating a more ordered peptide backbone, as predicted by MD simulations.

106 tion were recently discovered, the logic for peptide backbone assembly has remained a mystery.

107 Peptide backbone assignment and secondary structure pred

108 ntacts between the side chain of M35 and the peptide backbone at G33; (3) measurements of magnetic di

109 turbative strategy to probe hydration of the peptide backbone at specific depths within the bilayer u

110 (H-bond) between beta-chain His(81) and the peptide backbone at the -1 position is a candidate for s

111 s indicate a beta-strand conformation of the peptide backbone at the central phenylalanine.

112 interactions between the tip of eL4 and the peptide backbone at the end of TM10' participate in coor

113 e chains, and thus is presumably mediated by peptide backbone atoms.

114 s with the Erbin Val(1351) and displaces the peptide backbone away from the alpha-helix, elucidating

115 r, as the aromatic units are moved along the peptide backbone away from the hydrophobic core, the int

116 Along a defined peptide backbone, BA or CA residues are arranged to enab

117 promising nucleic acid mimetics in which the peptide backbone bears nucleobases.

118 The relaxation dynamics of the peptide backbone, beta-sheets and beta-turns, and negati

119 he Fe-N(epsilon)(2)His(F8)alpha1 bond to the peptide backbone bonds of residues His87(F8)alpha1 and A

120 ion (CAD) which, in addition to cleaving the peptide backbone bonds, cleaves the tag to produce repor

121 interacts with not only amide groups in the peptide backbone but also aliphatic groups, suggesting a

122 were actually N-glycopeptides with the same peptide backbone but different N-glycan compositions.

123 their ligands through interactions with the peptide backbone but do not distinguish between differen

124 atter contain an extra methylene unit in the peptide backbone but retain the original side chain.

125 is normally self-quenched by attachment to a peptide backbone but which can be activated by specific

126 ans in which the glycans are attached to the peptide backbone by entirely natural linkages.

127 arboxylic acids or amines separated from the peptide backbone by one to four CH2 groups.

128 d unit has been directly embedded within the peptide backbone by way of a synthetic amino acid with p

129 ermination show that a variety of alpha/beta-peptide backbones can adopt sequence-encoded quaternary

130 A large set of alpha/beta-peptide backbones can be generated by combining alpha- a

131 amide bond-a single atom substitution of the peptide backbone-can quench fluorophores that are red-sh

132 tide backbone particularly in cases when the peptide backbone cannot be identified by ETD/HCD.

133 i) This repulsion is transmitted through the peptide backbone, causing the movement of Asn 300.

134 ted in the deactivation of ecotin, caused by peptide backbone cleavage at its P1 reactive site.

135 CF-1 proteolytic repeat was shown to prevent peptide backbone cleavage, but whether aspartate glycosy

136 acid residue almost exclusively resulted in peptide backbone cleavage.

137 The peptide backbone, composed solely of both epitopes, was

138 e demonstrate that minimal alteration to the peptide backbone conformation occurs with aza-glycine in

139 of CsA do not originate from changes in the peptide backbone conformation.

140 of the Xaa side chains in the control of the peptide backbone conformation.

141 meric structures differ only slightly in the peptide backbone conformation.

142 l predictions, may generate a description of peptide backbone conformations at the residue level.

143 indicates a coil-alpha-beta-beta-alpha-coil peptide backbone, consistent with secondary-structure-pr

144 x)-Thr to P-selectin, demonstrating that the peptide backbone contributes to binding.

145 ith neighboring side-chain atoms or with the peptide backbone could be useful in therapeutic strategi

146 tes its fluorophore by promoting spontaneous peptide backbone cyclization and amino acid oxidation ch

147 ular biology tool because of its spontaneous peptide backbone cyclization and chromophore formation f

148 racterize GFP variants that not only undergo peptide backbone cyclization but additional denaturation

149 lational modification, with implications for peptide backbone cyclization in GFP, its homologues, and

150 The isomerizable azobenzene-peptide backbone defines the size and shape of the catal

151 ulfurization reaction) were carried out on a peptide backbone demonstrating the iterative nature of t

152 copeptides were attributable to 11 different peptide backbones, derived from IgG1, IgG2/3, IgG4, IgA1

153 tical hydrogen bonds between the MHC and the peptide backbone despite the presence of many proline re

154 Although the lack of the Phe-508 peptide backbone diminishes the NBD1 folding yield, the

155 , we find that electrostatic interactions of peptide backbone dipoles contribute significantly to the

156 cases are fast and quantitative and that the peptide backbones do not interfere with the self-assembl

157 so find that hydrogen bonding of urea to the peptide backbone does not play a dominant role in denatu

158 n unfavorable kink in the otherwise extended peptide backbone due to the presence of a prominent ridg

159 f the glycosidic bond occurring prior to the peptide backbone during collisionally activated dissocia

160 detailed picture of molecular events at the peptide backbone during unfolding and folding of CspA, w

161 alpha-carbon, providing direct detection of peptide backbone dynamics by electron paramagnetic reson

162 oxylic acid (TOAC) spin label, which reports peptide backbone dynamics directly.

163 hows rapid rotational motion consistent with peptide backbone dynamics of a locally unfolded peptide,

164 First, modifications of the peptide backbone (either N- or C-terminally, or both) wi

165 owever, the reaction mostly affords a linear peptide backbone, enabling post-Ugi transformations as t

166 ther catalytically active amino acids to the peptide backbone, enabling the stereoselective one-pot s

167 f coded and noncoded amino acid mutagenesis, peptide backbone engineering, and site-specific polymer

168 obtained by probing the amide I' band of the peptide backbone, exhibit nonexponential behavior and ar

169 lled by hydrophobic interactions between the peptide backbones, exposed to the solvent after partial

170 et of side-chain arrangements, even with the peptide backbone fixed in its crystallographic conformat

171 To delineate the role of peptide backbone flexibility and rapid molecular motion

172 research demonstrates that a small change in peptide backbone flexibility, which does not enhance pro

173 ese, the ability to efficiently sequence the peptide backbone for de novo identification, delineating

174 disulfide bond cleavages are preferred over peptide backbone fragmentation in ETD.

175 n of intact glycopeptides due to inefficient peptide backbone fragmentation when using collision-indu

176 lization but additional denaturation-induced peptide backbone fragmentation, native peptide hydrolysi

177 ragment ion series and facilitates extensive peptide backbone fragmentation.

178 .H-N hydrogen-bonded helices formed by other peptide backbones generated from alpha- and/or beta-amin

179 Moreover, by shielding the peptide backbone, glycans can block attempts to generate

180 that TFE acts by selectively desolvating the peptide backbone groups of the helix state.

181 s and orientations for (13)Calpha and (15)N (peptide backbone) groups in a protein, the beta1 IgG bin

182 The peptide backbone has a single predominant conformation.

183 nal restriction of side chain groups and the peptide backbone has yielded the most interesting result

184 cificity site (A site), which is effected by peptide backbone hydrogen bonds, a purine nucleotide sel

185 During the transition the peptide backbone hydrogen-bonding patterns were disrupte

186 ion of a hydrogen bond network constrain the peptide backbone in a way that makes it easier for the n

187 cosylation did not significantly perturb the peptide backbone in aqueous solution, but all four compo

188 ural transitions at specific sites along the peptide backbone in model beta-hairpin peptides.

189 nd as the initial point of attachment to the peptide backbone in mucin-type O-glycans.

190 f site-directed spin labeling and places the peptide backbone in the bilayer interfacial region and t

191 The flexibility of the peptide backbone in this 2D plane is reminiscent of intr

192 ter molecules, the hydrophilic residues, and peptide backbones in the transmembrane region is essenti

193 ed dissociation MS/MS fragmentation, and the peptide backbone information was provided by collision-i

194 ssessment, suggests a decreased nanoparticle-peptide backbone interaction and an increased contributi

195 This suggests differential insertion of the peptide backbone into the lipid bilayer.

196 ing that attack at the amide N-H bond in the peptide backbone is a highly viable pathway, which proce

197 glycan remains intact through ETD, while the peptide backbone is cleaved, providing the sequence of a

198 The peptide backbone is distinct from all previously charact

199 The S-shaped structure of the peptide backbone is formed by consecutive inverse gamma-

200 Because the peptide backbone is highly exposed to osmolyte in the de

201 d by the presence of PI(4,5)P2, and that the peptide backbone is positioned within the lipid interfac

202 The terminal cysteine thiol group on the PNA peptide backbone is reacted with a maleimide moiety on t

203 The overall conformation of the peptide backbone is similar between the two determinatio

204 he introduction of azole heterocycles into a peptide backbone is the principal step in the biosynthes

205 lpha) and C(beta) sites, indicating that the peptide backbone is unstructured.

206 iple site-specific glycosylation on the same peptide backbones is anticipated to have a significant i

207 es, a method we refer to as azoline-mediated peptide backbone labeling (AMPL).

208 chains inserted into the hydrocarbon and the peptide backbone lying within the bilayer interface.

209 Local constraints via peptide backbone methylation or preparation of cyclized

210 to modifications at every position along the peptide backbone, mimicking the specificity of the wild

211 We have now extended this peptide backbone N-methylation approach to a potent soma

212 Here, we describe the use of peptide backbone N-methylation as a new strategy to tran

213 fected the conformational equilibrium of the peptide backbone near the glycosylated Thr7 residue.

214 romatic units close to the N-terminus of the peptide backbone near the hydrophobic core of cylindrica

215 We show that the peptide backbone of an alpha-helix places a severe therm

216 uggesting that interactions of Mfa1 with the peptide backbone of BAR are important for binding.

217 stitutions in the residues that comprise the peptide backbone of ComX pheromone.

218 at binds specifically to sialic acid and the peptide backbone of glycophorin A on erythrocytes.

219 extent, sialylation as well as the sulfated peptide backbone of GSP-6' and GSP-6".

220 olide TE-802 is an excellent mimetic for the peptide backbone of macrocyclic HDACi.

221 The conformation of the peptide backbone of P450 2C19 is most similar to that of

222 etylglycine amide peptides as models for the peptide backbone of proteins, we set out to address thes

223 The peptide backbone of PVD is assembled by non-ribosomal pe

224 pathway of chromophore maturation, where the peptide backbone of residues 65-67 has condensed to form

225 s with the side chain of Lys-43 and with the peptide backbone of Ser-328 and Gly-329 from both subuni

226 The peptide backbone of the APDTRP fragment, which is a well

227 with hydrogen-bond interactions between the peptide backbone of the protease and that of the inhibit

228 We found that the peptide backbone of the substrate is anchored to the pro

229 from post-translational modification of the peptide backbone of three Cys and two Ser residues of th

230 Although the peptide backbones of 1-4 possessed random coil structure

231 discovered that the N-H stretches along the peptide backbones of alpha-helices can be detected in ch

232 nstead, a localized decrease in twist of the peptide backbone on the N-terminal side of the cysteine

233 recursor-specific while fragment ions of the peptide backbone originating from different labeling cha

234 neutralized by the dipoles of side-chain and peptide backbone oxygens rather than a formal negative c

235 s and lipoic acid were coupled to the 12-mer peptide backbones, PDC, a mutant PDC, and albumin.

236 rall agreement, the two structures differ in peptide backbone pitch and the orientation of several si

237 hus, these modified amino acids, in specific peptide backbones, play critical roles in their subunit-

238 tin variants suggest that dehydration of the peptide backbone plays a significant role in defining th

239 , such a simple chemical modification of the peptide backbone provides a useful conformational constr

240 tion number q for the EuL1 integrated into a peptide backbone, q = 0.96 +/- 0.09.

241 = 0.85) and the calculated hydration of the peptide backbone (r = 0.88).

242 isomer, binding of Fab partially stabilizes peptide backbone regions undergoing slow (microsecond to

243 l PTMs on PGC allows us to model them on the peptide backbone, revealing potential roles played by th

244 We conclude that involvement of the peptide backbone's carbonyl and amide groups in hydrogen

245 These interactions inhibit lactonization, a peptide backbone scission process that would normally be

246 Moreover, glycopeptides with an identical peptide backbone show nearly resembling spectra regardle

247 s, with little occurrence of dissociation at peptide backbone sites.

248 els, TOAC reports directly the motion of the peptide backbone, so quantitative analysis of its dynami

249 As found earlier for the peptide backbone, some perturbations found in the early

250 owed distinct structural propensities of the peptide backbone specific for either the nonglycosylated

251 ted that the 3Arg side chain orientation and peptide backbone stability each contribute significantly

252 -carbon, enabling direct detection by EPR of peptide backbone structural dynamics.

253 ct that the carbohydrate scaffold has on the peptide backbone structure and the role of the sugar in

254 rientation, and the resultant alterations in peptide backbone structure, affect a peptide's conformat

255 Rather than disrupting the peptide backbone structure, the protonated N-terminus se

256 h vibrations were used to determine the beta-peptide backbone structures for nine of the ten observed

257 The orientations of the two peptide backbone substituents and the phenyl group on th

258 tent, it appears that the orientation of the peptide backbone substituents on the cyclopropane rings

259 and the aromatic ring in 10 relative to the peptide backbone substituents on the cyclopropane were p

260 zole epsilon-amino acid and its utility as a peptide backbone substitute.

261 melittin has fewer cleavage sites along the peptide backbone than the larger conformer suggesting co

262 Residues 25-29 contain a bend of the peptide backbone that brings the two beta-sheets in cont

263 miting the conformational flexibility at the peptide backbone that is oxidized during red chromophore

264 rting significant structural rigidity to the peptide backbone that resulted in augmented protease res

265 ore includes derivatives of ornithine in the peptide backbone that serve as iron chelators.

266 ral vibrational modes and their couplings in peptide backbones that have been difficult to characteri

267 tion on the conformational propensities of a peptide backbone, the 15-residue peptide PPAHGVTSAPDTRPA

268 is inserted between the lipid anchor and the peptide backbone, thereby enabling light-triggered pepti

269 gy of the denatured state due to exposure of peptide backbone, thereby increasing the folding rate.

270 eracted directly with polar residues and the peptide backbone, thereby stabilizing nonnative conforma

271 e DNA bases and to the C(alpha) atoms of the peptide backbone (these are relatively rigid structural

272 ely, the single-atom, O-to-S modification of peptide backbone thioamidation has the potential to sele

273 rigid attachment of the metal chelate to the peptide backbone through both the amino acid side chain

274 formational freedom in water that allows the peptide backbone to adopt the major secondary structure

275 ions suggest that phosphorylation causes the peptide backbone to change direction and fold into a com

276 tryptophan and pyrene chromophores onto the peptide backbone to enable spectroscopic examinations of

277 er conformational change and exposure of the peptide backbone to proteolysis and angiostatin release.

278 in which the side chain is connected to the peptide backbone to provide control of chi(1)- and chi(2

279 ansition is due to the exposure of the polar peptide backbone to solvent upon helix unfolding.

280 ximity and an appropriate orientation of the peptide backbone to the tethered Fe-EDTA, was particular

281 are uniaxially averaged, suggesting that the peptide backbone undergoes uniaxial rotation around the

282 demonstrate additivity in DeltaG(tr) of the peptide backbone unit for all solvent systems studied.

283 issues and obtain DeltaG(tr) values for the peptide backbone unit.

284 sociated with enhanced dipole moments of the peptide backbone upon helix formation.

285 y the interaction of the Pd(II) ion with the peptide backbone upstream from the anchor.

286 sidue and that the modifications on the ComX peptide backbones vary in mass among the various pheroty

287 tional amino acids can be used in the cyclic peptide backbone, varying the structure and ring size of

288 hydrogen bond formation between urea and the peptide backbone, we predict that high urea concentratio

289 tion of side chains, and the position of the peptide backbone were observed.

290 Even in cases when the peptide backbones were correctly identified, the exact g

291 chains to segregate on opposite sides of the peptide backbone when it is in a fully extended beta-she

292 WG-4 kinks and stiffens the peptide backbone, which may hinder the interaction of su

293 favorable interaction between cosolvents and peptide backbones, which would be exposed to the cosolve

294 issociation of the N-C(alpha) bond along the peptide backbone while preserving the labile posttransla

295 While such constraints of the peptide backbone with disulfide bridges of different chi

296 e is a profound organizational effect on the peptide backbone with the alpha-linked glycans, attachme

297 porates a beta-lactam and an azapeptide in a peptide backbone with the intention of generating ration

298 in the side chain and the interaction of the peptide backbone with the surface.

299 ECD provided c and z. ions derived from the peptide backbone, with no observed loss of sugars.

300 Subsequent rearrangement cleaves the peptide backbone yielding a d-type fragment.