ライフサイエンスコーパス: polypeptide chain

1 ously tested Shigella antigens into a single polypeptide chain.

2 related structures and includes the complete polypeptide chain.

3 Pasteurella heparosan synthases in a single polypeptide chain.

4 ing state or contain a defined translocating polypeptide chain.

5 s several distinct functions within a single polypeptide chain.

6 of an IgG1 and at multiple sites in the same polypeptide chain.

7 oglutamate can form on the N terminus of the polypeptide chain.

8 domain (DBD) occur multiple times within one polypeptide chain.

9 se domain, and a protease domain, all in one polypeptide chain.

10 ive molecular motion for the majority of the polypeptide chain.

11 are similar to those imposed on the nascent polypeptide chain.

12 increase the rigidity and compactness of the polypeptide chain.

13 mains present adjacent to each other along a polypeptide chain.

14 ching through different conformations of the polypeptide chain.

15 nce, but rather to the mature portion of the polypeptide chain.

16 and transfers an Ala residue to the growing polypeptide chain.

17 chain connected by linkers to form a single polypeptide chain.

18 the characteristics of a completely unfolded polypeptide chain.

19 llow the passive directional movement of the polypeptide chain.

20 -ene and dioxygen) are derived from the same polypeptide chain.

21 hich we localize to specific segments of the polypeptide chain.

22 l transferase center to release the finished polypeptide chain.

23 of conformational movements within a single polypeptide chain.

24 6-aa Cys peptide, to yield the target 130-aa polypeptide chain.

25 multiple cellular functions within a single polypeptide chain.

26 rminal adenosine for addition to the growing polypeptide chain.

27 e molecular level, in the coil states of the polypeptide chain.

28 ibosome exerts a destabilizing effect on the polypeptide chain.

29 n9GlcNAc2 oligosaccharides as well as to the polypeptide chain.

30 y a long intrinsically disordered N-terminal polypeptide chain.

31 tryptophan at different locations along the polypeptide chain.

32 ociated with the signal-transducing FcRgamma polypeptide chain.

33 wn function (DUF) near the C terminus of the polypeptide chain.

34 -tryptophan variants encompassing the entire polypeptide chain.

35 ependent structural or functional units of a polypeptide chain.

36 space of folded structures accessible to the polypeptide chain.

37 ment that precedes the fusion peptide in the polypeptide chain.

38 ut because it forms a nanopore from a single polypeptide chain.

39 e efficiently performed by components of the polypeptide chain.

40 bunit is composed of one CL-L1 and two CL-K1 polypeptide chains.

41 the tight interleaving of their constituent polypeptide chains.

42 electrostatic interactions between adjacent polypeptide chains.

43 with the rate of formation differing between polypeptide chains.

44 ed with processes that involve misfolding of polypeptide chains.

45 ion of full-length, chemically denatured GFP polypeptide chains.

46 es that mediate the ATP-dependent folding of polypeptide chains.

47 ed with secondary structure formation of the polypeptide chains.

48 increase of the number of GABs on individual polypeptide chains.

49 mutual synergistic folding of two disordered polypeptide chains.

50 e ribosome through an exit tunnel as nascent polypeptide chains.

51 sfer occurs between active sites on separate polypeptide chains.

52 e, facilitating its interaction with nascent polypeptide chains.

53 -DP molecules genetically linked into single polypeptide chains.

54 t restrict the conformational freedom of the polypeptide chains.

55 ter reproductions of the local structures of polypeptide chains.

56 ms the binding interface between interacting polypeptide chains.

57 signal peptide produces N-terminal elongated polypeptide chains.

58 ng templates, such as properly folded DNA or polypeptide chains.

59 in to Levinthal's paradox for the folding of polypeptide chains.

60 ns seems to constitute a generic property of polypeptide chains.

61 ith the inherent aggregation propensities of polypeptide chains.

62 tively affected the retention of most of the polypeptides chains.

63 nsights into the conformational passage of a polypeptide chain across its free energy landscape have

64 The polypeptide chain adopts the typical alphabetaalpha PTP

65 mprising 51 residues in two disulfide-linked polypeptide chains, adopts a predominantly alpha-helical

66 re located in different positions within the polypeptide chains, alignment of their structures show t

67 complex Gordian knot topology formed by the polypeptide chain alone.

68 is sp. is heterodimeric, with two homologous polypeptide chains, alpha and beta, derived from a commo

69 Hsp70 that binds ribosome-associated nascent polypeptide chains, also binds to the TPR domain of Sec7

70 els considering the net global charge of the polypeptide chain, although the kinetics of the process

71 f proteins, stabilizing domains, and linking polypeptide chains, although some cases of extracellular

72 known about spontaneous knot formation in a polypeptide chain-an event that can potentially impair i

73 mical protein synthesis to prepare three ShK polypeptide chain analogues, each containing either an a

74 l protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic m

75 acteria and eukaryotes, consists of a single polypeptide chain and contains three major domains: the

76 ification entails partial duplication of the polypeptide chain and mutation of a key catalytic residu

77 that shows users the knot type of the entire polypeptide chain and of each of its subchains.

78 0 particle images, shows the trace of the L1 polypeptide chain and reveals how the N- and C-terminal

79 Although the overall fold of the polypeptide chain and the oligomeric state of this prote

80 Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modu

81 ans, formed from sequentially non-homologous polypeptide chains and affecting human or animals.

82 Oligomeric interactions between Ca-ATPase polypeptide chains and their modulation by phospholamban

83 ystallography allowing tracing of structural polypeptide chains and visualization of transmembrane pr

84 functional interactions between neighboring polypeptide chains and, in turn, result in increased rat

85 simulations were started from fully extended polypeptide chains, and no external information was incl

86 cular forces responsible for configuring the polypeptide chain are also changed.

87 inct from the fibril lattice even though the polypeptide chains are organized in an immunologically i

88 No functional human beta globin polypeptide chains are produced.

89 ngly facilitated incorporation of Ser in the polypeptide chain as compared with selenocysteine at the

90 hat the coarse-graining of the structures of polypeptide chains as self-avoiding tubes can provide an

91 factor (TF) interacts directly with nascent polypeptide chains as they emerge from the ribosome exit

92 RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA.

93 ic interactions between various sites in the polypeptide chain, as would occur during the initiation

94 nal Ag-presentation pathways via unprocessed polypeptide chains, as free IGRP206-214 peptide or via p

95 ollagen C-propeptide trimer, where the three polypeptide chains associate together, at the junction w

96 es also revealed a well ordered break in the polypeptide chain at Lys(147), resulting in a large conf

97 Caspase-3 cleaves the polypeptide chain at the exposed DEVD motif; however, th

98 FAD and FMN binding domains within a single polypeptide chain, bacterial NOS is only composed of an

99 signal recognition particle (SRP) recognizes polypeptide chains bearing a signal sequence as they eme

100 It is now clear which polypeptide chains become disordered and which become re

101 c binding event between compact and flexible polypeptide chains being the initial step.

102 mpanied by a fission of the radical-carrying polypeptide chain between the Gly436 and His437 residues

103 erone family are capable of interacting with polypeptide chains both co- and posttranslationally, but

104 The channel itself does not bind the polypeptide chain but provides "friction" that minimizes

105 ular interactions between the fibril-forming polypeptide chains, but it has so far remained difficult

106 athway: the ongoing synthesis of the nascent polypeptide chain by the ribosome.

107 could generate all three domains as separate polypeptide chains by thrombin treatment in vitro.

108 ammals the enzymes are expressed as a single polypeptide chain (CAD) in the order CPS-DHO-ATC and ass

109 hesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that i

110 ich contains a number of routes by which the polypeptide chain can convert its primary sequence into

111 To help solve the puzzle of how a polypeptide chain can efficiently knot itself, the foldi

112 he confinement of the chaperonin cavity, the polypeptide chain cannot undergo aggregation but rather

113 a heterodimer of 18 to 19 kDa composed of 2 polypeptide chains, CL2 and AL.

114 residue hydrophilic, unstructured N-terminal polypeptide chain comprising proline, alanine, and serin

115 at of an overall extended and highly dynamic polypeptide chain comprising three helical segments and

116 as a "cupin" fold, extremely similar both in polypeptide chain conformation and in dimer geometry to

117 well as the effects of the properties of the polypeptide chain connecting the contiguous domains, are

118 -terminal domain and is composed of a single polypeptide chain containing fragment 2 (residues 156-27

119 Interactions between polypeptide chains containing amino acid residues with o

120 ind that the topological organization of the polypeptide chain critically determines the folding coop

121 tional translocation, the ribosome feeds the polypeptide chain directly into the channel.

122 The resulting truncated BdlA polypeptide chains directly interact and are required fo

123 nd addition of the amino acid to the growing polypeptide chain during protein synthesis.

124 Sec is incorporated into the growing polypeptide chain during translation elongation and is k

125 le is known about the progressive folding of polypeptide chains during chain synthesis by the ribosom

126 it the conformational space available to the polypeptide chains during misfolding and fibrillization.

127 including cotranslational folding of nascent polypeptide chains during their synthesis by the ribosom

128 (EF2K), which inhibits elongation of nascent polypeptide chains during translation.

129 In addition to its roles in polypeptide chain elongation, unique cellular and viral

130 n pausing, roughly at the site where nascent polypeptide chains emerge from the ribosomal exit tunnel

131 gnal recognition particle (SRP) when nascent polypeptide chains emerge from the ribosome.

132 the 5-fold axis; residues 81-100 link the 10 polypeptide chains emerging from a 5-fold hub to the N-t

133 g, including the balance between solvent and polypeptide chain entropies.

134 Do polypeptide chains ever behave like a random coil?

135 hosphorylation of PLB, neighboring Ca-ATPase polypeptide chains exhibit a 4 +/- 2 A decrease in the p

136 ange of experimental techniques suggest that polypeptide chains expand with increasing denaturant con

137 assess the internal scaling behavior of the polypeptide chain, expressed as a mass fractal dimension

138 ominent feature of this fold, as well as the polypeptide chain fold of an amyloid structure.

139 The synthetic ester insulin polypeptide chain folded much more rapidly than proinsul

140 domain initiates with an extended region of polypeptide chain followed by two turns of an amphipathi

141 ting with the DNA-binding domain on the same polypeptide chain for a cis interaction.

142 n aberrant, translationally arrested nascent polypeptide chains for proteasomal degradation.

143 n and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation.

144 We consider the mechanical stretching of a polypeptide chain formed by multiple interacting repeats

145 formation about protein structures with open polypeptide chains forming knots or slipknots.

146 The 63-residue En-6 polypeptide chain forms three alpha-helices in positions

147 bacteriophage T4 is synthesized as a single polypeptide chain from a discontinuous reading frame as

148 hesizing factories of the cell, polymerizing polypeptide chains from their constituent amino acids.

149 The chemical synthesis of polypeptide chains >50 amino acids with prescribed seque

150 ing NMR spectroscopy, we show that the PAGE4 polypeptide chain has local and long-range conformationa

151 plings between amino acids within and across polypeptide chains have allowed for inference of native

152 Knots in polypeptide chains have been found in very few proteins,

153 position, which is expected for an extended polypeptide chain having little or no propensity to form

154 kinetics of formation of end-to-end loops in polypeptide chains; however, protein folding more often

155 ) and BsmI/Mva1269I (GAATGC 1/-1) are single polypeptide chains, i.e. monomers, rather than heterodim

156 The regions of the polypeptide chain immediately preceding or following an

157 constrains the conformations of the nascent polypeptide chain in a manner not experienced by full-le

158 myloids consist of repetitions of a specific polypeptide chain in a regular cross-beta-sheet conforma

159 lory exponent (nu) of the thermally unfolded polypeptide chain in both states.

160 onotonic trend between the dimensions of the polypeptide chain in bulk and the degree of compaction:

161 ther, these data suggest that SecA binds the polypeptide chain in its ATP state and releases it in th

162 observe simultaneous folding of the nascent polypeptide chain in real time.

163 erage conformational degeneracy of a lattice polypeptide chain in water and quantitatively show that

164 kbone and side chain conformational space of polypeptide chains in a united-residue representation an

165 role in the folding and assembly of nascent polypeptide chains in the ER.

166 616 non-interface residues extracted from 99 polypeptide chains in the Protein Data Bank.

167 We have traced the VP7 polypeptide chain, including parts not seen in its X-ray

168 n permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side

169 The availability of the eukaryotic polypeptide chain initiation factor 4E (eIF4E) for prote

170 Spontaneous folding of a polypeptide chain into a knotted structure remains one o

171 se that the two-helix finger of SecA moves a polypeptide chain into the SecY channel with the tyrosin

172 ong bacteria, which converts Arg residues in polypeptide chains into citrulline.

173 ructure--the ordered aggregation of separate polypeptide chains into multisubunit assemblies.

174 rectly modifying, folding and assembling the polypeptide chains into the native quaternary structure.

175 s simulations revealed that ESI for unfolded polypeptide chains involves protein ejection from nanodr

176 How the polypeptide chain is able to "knot" itself during the fo

177 ks via linker sequences into one multivalent polypeptide chain is an elegant alternative to affinity

178 approximately 13 amino acid residues as the polypeptide chain is apparently shortened by approximate

179 uential addition of amino acids to a growing polypeptide chain is carried out by the ribosome in a co

180 donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltrans

181 he compact packing typical of a fully folded polypeptide chain is disrupted and suggest that the incr

182 ect to the distance between hemes, along the polypeptide chain is exactly the same in both redox syst

183 During co-translational folding, the nascent polypeptide chain is extruded sequentially from the ribo

184 ns explored and show that this region of the polypeptide chain is involved in both the nucleation and

185 SecY complex raises the possibility that the polypeptide chain is moved by a two-helix finger domain

186 The knotted/slipknotted polypeptide chain is one of the most surprising topologi

187 ore unusually, the N-terminal portion of the polypeptide chain is pinned to the "Kunitz head" by two

188 ng a covalent-loop through which part of the polypeptide chain is threaded (as seen in knotted protei

189 tides are moved by different mechanisms: the polypeptide chain is transferred directly into the chann

190 cid from a non-cognate tRNA into the growing polypeptide chain leads to a general loss of specificity

191 We show that by varying polypeptide chain length and dendron generation, an orga

192 named insulin-like 3 (INSL3) consists of two polypeptide chains linked by two interchain and one intr

193 omplexes between the ligand and the extended polypeptide chain may act as nucleation sites for foldin

194 et been resolved, but the arrangement of the polypeptide chain may have a strong influence on the cap

195 te that tunnel interactions with the nascent polypeptide chain might be relevant for the regulation o

196 that targets the associated mRNA and nascent polypeptide chain (NC).

197 m a trefoil knot in the denatured state of a polypeptide chain of 120 residues is 5.8 +/- 1 kcal mol(

198 threonine protein kinase comprising a single polypeptide chain of 4,128 amino acids and belonging to

199 sistent with a model for repair in which the polypeptide chain of a DPC is first reduced by proteolys

200 d the potential benefits of reorganizing the polypeptide chain of a protein by circular permutation (

201 e internal redox steps occur within the same polypeptide chain of mammalian QSOX and commence with a

202 The polypeptide chain of rabbit uterine smMLCK (Swiss-Prot e

203 The predicted 81 amino acid residue polypeptide chain of sfAFP contains Cys residues at posi

204 The target 148 residue polypeptide chain of sortase ADeltaN59 was synthesized b

205 th both TS and DHFR active sites on a single polypeptide chain of the enzyme.

206 The 130-aa wild-type polypeptide chain of the human enzyme was assembled from

207 Ac residue to alpha-GalNAc residue along the polypeptide chain of Tn-PSM before dissociating.

208 The vicilin consisted of two polypeptide chains of about 43 and 45 kDa in size when a

209 d significantly slower cleavage of all three polypeptide chains of fibrin from patients compared with

210 was identified within ribosomally expressed polypeptide chains of four conopeptides from the venoms

211 The polypeptide chains of FrhB, for which there was no homol

212 The entire polypeptide chains of GKalphabeta are structurally defin

213 d superfamily of ion channels are encoded as polypeptide chains of six transmembrane-spanning segment

214 The two polypeptide chains of the erythroid spectrin heterodimer

215 We found that the C-tails of the two polypeptide chains of the rat Abeta(1-16) dimer are orie

216 1q is a hexameric molecule assembled from 18 polypeptide chains of three different types encoded by t

217 Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt

218 f multifunctional proteins in which a single polypeptide chain performs multiple biochemical function

219 tions, such as the formation of loops in the polypeptide chain, places one physical limit on the spee

220 olvent accessible surface area (SASA) of the polypeptide chain plays a key role in protein folding, c

221 The assumption is that unfolded polypeptide chains possess an intrinsic propensity to fo

222 is a heterodimer consisting of 2 homologous polypeptide chains, PPO1 and PPO2.

223 is is the first evidence that folding of the polypeptide chain precedes disulfide formation within a

224 e ring forms a 'gasket-like' seal around the polypeptide chain, preventing the permeation of small mo

225 f Arc repressor, a region of Arc repressor's polypeptide chain previously shown to have other non-nat

226 Propagation of the polypeptide chains proceeds through the transfer of the

227 h consists of disulfide cross-linked A and B polypeptide chains, readily forms amyloid fibrils under

228 m and determine the role of its two distinct polypeptide chains, recombinant holo-ACL as well as its

229 in the central region of phospho-PAGE4, the polypeptide chain remains highly dynamic overall.

230 ons of two opposite topologies from the same polypeptide chain remains unclear.

231 specifically an aromatic-rich region of the polypeptide chain (residues 62-70) that has been predict

232 xpression of the corresponding complementary polypeptide chains, retain tetrameric architecture and a

233 er of Escherichia coli SecA interacts with a polypeptide chain right at the entrance into the SecY po

234 e TRAIL protomers were expressed as a single polypeptide chain (scTRAIL), and a novel TRAIL variant,

235 e formation of beta-sheet structures, as the polypeptide chain searches for the native stabilizing cr

236 caffeate acts by disordering precisely those polypeptide chain segments that make up the active site

237 e disulfides spanning a large portion of the polypeptide chain shifts the structure and dynamics of h

238 Simulations in the presence of a polypeptide chain show that the substrate associates wit

239 the plastid envelope and the importing PORA polypeptide chain such that no photoexcitative damage oc

240 any proteins contain regions of unstructured polypeptide chain that appear to be flexible and to unde

241 re conducted using a single monomer gammaTIM polypeptide chain that folds as a monomer and two gammaT

242 Human serum transferrin (hTF) is a single polypeptide chain that folds into two lobes (N- and C-lo

243 Thus, the proportion of polypeptide chain that is locally and presumably transie

244 rus genome is translated to produce a single polypeptide chain that subsequently is cleaved by viral

245 he excluded volume of a local segment of the polypeptide chain that transiently stalls in the nanopor

246 onformationally restricted in regions of the polypeptide chain that ultimately form helices I, II and

247 BoNTs are synthesized as single inactive polypeptide chains that are cleaved by endogenous or exo

248 al machineries for the synthesis of thirteen polypeptide chains that are components of the complexes

249 matic, because immune receptors comprise two polypeptide chains that are encoded by separate mRNAs.

250 rring proteins are not general properties of polypeptide chains that fold to unique stable structures

251 but also several further versions of the two polypeptide chains that most likely differ with respect

252 sting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid f

253 Collagens are composed of three polypeptide chains that wind into triple helices.

254 MCM2-7 is a heterocomplex made of different polypeptide chains, the MCM complexes of many Archaea fo

255 n, because sortase A enables the splicing of polypeptide chains, the transpeptidation reaction cataly

256 roEL-GroES sterically confines the unknotted polypeptide chain thereby promoting knotting is unlikely

257 s protein synthesis by accepting the growing polypeptide chain, thereby killing bacterial cells.

258 ding nucleators by preorganizing the pendant polypeptide chains, thereby lowering the activation barr

259 h a nontranslocating SecY copy and moves the polypeptide chain through a neighboring SecY copy.

260 ich ATP hydrolysis by SecA is used to move a polypeptide chain through the SecY channel.

261 suggests a dimeric arrangement of Ca-ATPase polypeptide chains through the proximal association of N

262 lectively oxidizes the N-terminal amine of a polypeptide chain to a ketone or an aldehyde group.

263 te modulates the intrinsic propensity of the polypeptide chain to aggregate and that the algorithm de

264 cause the protein slipknot to untie and the polypeptide chain to completely extend.

265 lix motifs) facilitate bending and allow the polypeptide chain to fold into a hollow circular structu

266 binding provides a major driving force for a polypeptide chain to fold.

267 coarse-grained C(alpha)-side chain model for polypeptide chains to simulate the folding of src SH(3)

268 tudied folding events at the early stages of polypeptide chain translocation into the mammalian ER us

269 alent folding and assembly of macromolecular polypeptide chains, ultimately preventing the formation

270 haracterize the crowding effects on the same polypeptide chain under two drastically distinct folding

271 It is generally held that random-coil polypeptide chains undergo a barrier-less continuous col

272 c stabilities and m-values, we show that the polypeptide chain undergoes rapid collapse to an interme

273 Essentially the entire MeCP2 polypeptide chain underwent H/DX at rates faster than co

274 n a substrate and then translocate along the polypeptide chain, unfolding and degrading protein domai

275 of tension propagation and relaxation of the polypeptide chain upon force quench.

276 f the chaperone machinery that binds nascent polypeptide chains upon their exit from the ribosome, Jj

277 ecause of simplified UNRES representation of polypeptide chains, use of enhanced sampling methods, co

278 Type 2 RIPs contain two polypeptide chains (usually named A, for "activity", and

279 The iron hemes of MtrA are bound to its polypeptide chain via proximal (CXXCH) and distal histid

280 The synthetic polypeptide chain was folded in vitro into a defined ter

281 or and acceptor fluorescent dyes on the same polypeptide chain, was developed.

282 he interactions between the nanopore and the polypeptide chain we have obtained results that are rele

283 and allo-Ile, both l-allo-ShK and d-allo-ShK polypeptide chains were prepared by total chemical synth

284 forming Met66 residue is eliminated from the polypeptide chain, whereas Leu66 in Blue102 is cleaved o

285 and P-domain elements of proximal Ca-ATPase polypeptide chains which restore functional interactions

286 of a flexible, scaled, physical model of the polypeptide chain, which accurately reproduces the bond

287 mic model for nearly all of the 2109-residue polypeptide chain, which comprises three enzymatic domai

288 synthesis to make the central segment of the polypeptide chain, which forms the transmembrane beta-ba

289 eral copies of the cruciferin alpha and beta polypeptide chains, which are present in various isoform

290 -puro forms covalent conjugates with nascent polypeptide chains, which are rapidly turned over by the

291 o-acid sequence result in shorter or cleaved polypeptide chains while the incomplete processing of th

292 le-chain trimers (SCTs) composed of a single polypeptide chain with a linear composition of antigenic

293 ies of cyanovirin-N that all are formed by a polypeptide chain with the identical amino acid sequence

294 isms as well as the interactions of unfolded polypeptide chains with other cell components.

295 n only be measured at high concentrations of polypeptide chains with slow scanning rates, for example

296 tide self-assembly to deliver extremely long polypeptide chains with stipulated, repeated sequences.

297 le of hindered dihedral rotations within the polypeptide chain, with a proportionality coefficient b

298 ulation increased, signaling collapse of the polypeptide chain, with protein L being slightly more co

299 During protein synthesis, nascent polypeptide chains within the ribosomal tunnel can act i

300 her (lanthionine) cross-links within nascent polypeptide chains, yielding macrocyclic proteins with p