ライフサイエンスコーパス: amino acid side chain

1 eta-signal motif depend on the nature of the amino acid side chain.

2 which carries a reactive azide moiety in its amino acid side chain.

3 h between a pendant group of a base with the amino acid side chain.

4 partially compensate for differences in the amino acid side chain.

5 AP, by the absence of the amine group on the amino acid side chain.

6 nd involves the detailed architecture of the amino acid side chain.

7 basis of the size and hydrophilicity of the amino acid side chain.

8 to account the known intrinsic reactivity of amino acid side chain.

9 the protein proximal ADP-ribose and a given amino acid side chain.

10 depending on the polarity of the position 74 amino acid side chain.

11 a very narrow tunnel, which excludes larger amino acid side chains.

12 t undergo motional averaging such as that of amino acid side chains.

13 solvent accessible surface area (<SASA>) of amino acid side chains.

14 do moiety and its apposition to the reactive amino acid side chains.

15 with the concomitant exposure of hydrophobic amino acid side chains.

16 uctural information encoded in a sequence of amino acid side chains.

17 ng internal water molecules along with polar amino acid side chains.

18 yl-containing, post-translationally modified amino acid side chains.

19 ct of multiple bp by conformationally mobile amino acid side chains.

20 enaturation was much slower with hydrophobic amino acid side chains.

21 e distribution and local topology of charged amino acid side chains.

22 of the core region of MRP1 that includes the amino acid side chains.

23 local environments to tune the reactivity of amino acid side chains.

24 ol) binding by the membrane insertion of its amino acid side chains.

25 ructure via altered solvent accessibility of amino acid side chains.

26 displaying both hydrophobic and hydrophilic amino acid side chains.

27 ostatic properties of the enzyme active site amino acid side chains.

28 c forces imposed by the presence of nonpolar amino acid side chains.

29 teractions are possible for all the aromatic amino acid side-chains.

30 allowing for small (1.0 A) movements in the amino acid side-chains.

31 ical properties and relative position in the amino acid side-chains.

32 atalyst capable of modifying a wide range of amino-acid side chains.

33 es with similar chemistries to the wild-type amino acids' side chains.

34 tep electron tunneling in which redox-active amino acid side chains act as intermediate donors or acc

35 to the reversible light-switching of single amino acid side-chains, adding a dynamic dimension to pr

36 To investigate how structural changes in the amino acid side chain affect nucleotide substrate select

37 The imidazole group of histidine is the only amino acid side chain affected within this range.

38 Second, free energy profiles for transfer of amino acid side chains along the normal to a phosphatidy

39 sily detectable products for all 20 (common) amino acid side chains along with cystine are directly c

40 favorable interactions with the hydrophobic amino acid side chain, alpha-carbon, carboxylate, and th

41 actions between the bases in the DNA and the amino acid side chains also differ from those observed i

42 hine and all standard, non-glycyl/non-prolyl amino acid side chain analogs as derived from molecular

43 ute, independent synthesis of the N-terminal amino acid side chain and a stereoselective de novo cons

44 esently limited by the repertoire of natural amino acid side chain and carbohydrate functionalities.

45 ate to the peptide backbone through both the amino acid side chain and coordination of the amide carb

46 Our results indicate that the amino acid side chain and identity of the olefin profoun

47 ally, demonstrating the key role of both the amino acid side chain and the catalytic bromide anion.

48 onding interactions with several surrounding amino acid side chains and a water molecule, P(B) does n

49 r of direct hydrogen bonds between conserved amino acid side chains and bases.

50 roups, including proton-exchanging groups of amino acid side chains and bound water molecules.

51 he formation of covalent cross-links between amino acid side chains and DNA bases in DNA-protein comp

52 In addition, their attraction to acidic amino acid side chains and formation of a hydrogen bond

53 ism reconfigures atomic interactions between amino acid side chains and internal water in an unusual

54 In this study, the specific role of amino acid side chains and molecular processes involved

55 caused by the perturbation of several polar amino acid side chains and several internal water molecu

56 by disruption of the cluster of hydrophobic amino acid side chains and that the midregion of the coi

57 relation between the hydrophobicity index of amino acid side chains and the binding affinity and dena

58 ning the consequences of truncating specific amino acid side chains and the effects of these truncati

59 base-stacking interactions between aromatic amino acid side chains and the substrate.

60 However, specificity for different amino acid side chains and the tRNA body is observed whe

61 n order to determine the ionization state of amino acid side chains and their pK(a)s.

62 We include dynamic fluctuations of amino acid side chains and water molecules into our anal

63 ic interactions between the bound ligand and amino acid side chains and/or changes in heme stereochem

64 tidine is dependent on both the length of an amino acid side-chain and the identity of terminal funct

65 rt, by hydrogen bonding interactions between amino acid side-chains and nucleotide bases.

66 The ligands contain a tertiary amine, an amino acid side chain, and a carbamate or amide function

67 functionalization of the Zn(2+)-coordinating amino acid side chain, and alkylation of the backbone am

68 from changes of protein backbone, substrate, amino acid side chain, and cofactor vibrations.

69 tivity, 2'-regioselectivity, independence of amino acid side chain, and phosphorylated activating gro

70 the fluorophores were incorporated into the amino acid side chains, and both probes [1 and L-(7-hydr

71 Phosphorylation adds negative charge to amino acid side chains, and negatively charged amino aci

72 ould be identified for more than half of the amino acid side chains, and site-specific assignments we

73 arch space of degrees of freedom of ligands, amino acid side chains, and the protein backbone.

74 contacts beta at this site, but not through amino acid side chains, and thus is presumably mediated

75 modulated by interactions involving charged amino acid side chains; and 7) Norrin-CRD binding is enh

76 ions in solid state NMR signals from certain amino acid side chains are also observed, suggesting dif

77 ligands, prosthetic groups, and protein and amino acid side chains are found.

78 Several hydrophobic amino acid side chains are positioned near the polyisopr

79 o 193 of FNR was utilized to determine which amino acid side chains are required for transcription of

80 Gdm(+) can interact with a number of planar amino-acid side chains (Arg, Trp, Gln) in a stacking man

81 dditional water molecules bind either to the amino acid side chain as in tyrosine or to already-bound

82 covalently bound heme that does not possess amino acid side chains as axial ligands.

83 xes show distinct bands that may result from amino acid side chains as well as structural changes in

84 anticodon encodes the hydrophobicity of each amino acid side-chain as represented by its water-to-cyc

85 co-translationally modified to give a novel amino acid side chain, aspartyl aldehyde.

86 This variant allele (C382R) alters an amino acid side chain at a principal interface between t

87 amide at C3 (beta-lactam numbering) and the amino acid side chain at C4 are well-tolerated, allowing

88 xy-2-azetidinone is used to install the beta-amino acid side chain at the C-5' position of the carboc

89 that a subtle difference in the size of the amino acid side chain at this position has a significant

90 e protein backbone, but movements of several amino acid side chains at the binding site, in particula

91 Amino acid side chains at the helix-helix interface of a

92 del has been that TEA is coordinated by four amino acid side chains at the position equivalent to Sha

93 rations of the charge, polarity, and size of amino acid side chains at these sites alter the ability

94 calculated free energies of partitioning of amino acid side chains between water and alkane yielded

95 of a deep cleft, heavily lined with aromatic amino acid side-chains but bounded by numerous charged g

96 f proteins are posttranslationally modified: amino acid side chains can be modified, peptide bonds ca

97 nstructured portion of Scr so that two basic amino acid side chains can insert into the minor groove

98 within the membrane interfacial region where amino acid side chains can interact with phospholipid he

99 main; homology modeling suggests that mutant amino acid side chains can potentially fill the cleft be

100 ed benzene rings (a simple model of aromatic amino acid side chains) can switch inherent dynamical te

101 as indicated by variation in composition of amino acid side chain category.

102 Due to the similarity in many amino acid side chains, certain synthetases misactivate

103 lement of amino acids, determined largely by amino acid side-chain charge.

104 an amino-acid within a motif, correlation of amino-acids side-chain charges within a motif and Ramach

105 determined rates of proteolytic cleavage and amino acid side chain chemical modifications in native,

106 and explores the synergistic contribution of amino acid side-chain chemistry.

107 les; however, the correct orientation of the amino acid side chains (chi-space) that constitute the p

108 Strong contribution of the aromatic amino acid side chain chromophores to the far-UV circula

109 hotolysis that react with a broader range of amino acid side chains compared with the benzophenone-de

110 all the structures were similar, significant amino acid side chain conformational rearrangements were

111 nance (NMR), with significant differences in amino acid side chain conformations and helix 9-helix 9

112 Rotamer analysis of amino acid side-chain conformations indicated that 2 var

113 in dimer with its RNA operator reveals eight amino acid side-chains contacting seven of the RNA phosp

114 It has previously been noted that many amino acid side chains contain considerable nonpolar sec

115 AMPA-Rs is controlled by the identity of the amino-acid side chain contributed by each subunit at a k

116 fore indicate that the steric nature of this amino acid side chain contributes to stabilization of th

117 include (i) the possibility of incorporating amino acid side chains corresponding to many of the prot

118 suggests that the flexibility of individual amino acid side chains could be important in determining

119 exploits the so-called anchor residues, i.e. amino acid side-chains deeply buried at protein-protein

120 A growing body of evidence suggests that amino acid side chains dramatically influence amyloid fo

121 echanism involving nucleophilic attack of an amino acid side chain (e.g. the epsilon-amino group of l

122 te that relatively minor changes in a single amino acid side chain (e.g., alanine to valine or glutam

123 attack on the imine by a second nucleophilic amino acid side chain, e.g., from serine 130, to form a

124 generally situated such that the respective amino acid side chains either project into the predicted

125 ng to the beta3 cytoplasmic domain increased amino acid side chain embedding at the inner and outer b

126 Others have proposed that several amino acid side chains exhibit considerable conformation

127 Mutation of amino acid side chains exposed in a putative peptide-bin

128 and tunnel" and shows that several important amino acid side chains extrude into the solvent instead

129 37.4 kcal/mol; (2) that alkyl groups on the amino acid side chains favor helix formation even in the

130 lative accessibility of the nitroxide-tagged amino acid side chains for the solubilized COX-2 mutants

131 ough minor adjustment of the rotamers of two amino acid side chains for this latter structure, a mode

132 estigated the effects of changing the A-site amino acid side chain from phenylalanine to alanine.

133 The target displays the key amino acid side chains from a novel tricyclic scaffold.

134 d 84 mutations due to the alterations in the amino acid side chains from longer to shorter (e.g., V82

135 transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilaye

136 The reactive and solvent-accessible amino acid side chains function as structural probes; ho

137 etween 6A6 and tissue factor at the level of amino acid side-chain functional groups.

138 these alcohols induces perturbations in the amino acid side-chain gates linking pairs of cavities, a

139 ND(3)-mediated HDX at peptide termini and amino acid side chains goes to completion within 1 s.

140 Thus a fluxional process for a metal-bound amino acid side chain has now been identified.

141 Aromatic amino acid side chains have a rich role within proteins

142 eractions between carbohydrates and aromatic amino acid side chains, however, are supplemented by CH-

143 locally orient the peptide backbone and the amino acid side chain in a predefined manner.

144 The role of the amino acid side chain in enzymes with Glu/Gln/Ala substi

145 the activity of an Rrp6 mutant lacking a key amino acid side chain in its active site.

146 f a modulatory, nontransported proton to the amino acid side chain in position 295.

147 guous evaluation of the kinetic role of each amino acid side chain in the catalyst.

148 ate the average solvent accessibility of the amino acid side chain in the folded protein.

149 ves as an H-bond donor to an electronegative amino acid side chain in the SH1 binding site.

150 e we present a chemical technique to oxidize amino acid side chains in a model protein, apomyoglobin,

151 l studies have identified many intercalating amino acid side chains in a wide variety of enzymes, but

152 hment of a single ortho position of aromatic amino acid side chains in an otherwise perdeuterated bac

153 assessment of the roles played by different amino acid side chains in creating the high-affinity, hi

154 elated with drug-induced localized shifts of amino acid side chains in CYP46A1 and unusual interactio

155 These data suggest that none of the amino acid side chains in helix 9 is absolutely required

156 Conserved amino acid side chains in Ire1 that face into the groove

157 the alpha position to the ester, resembling amino acid side chains in peptide substrates, impacted C

158 uently, free energies of interaction between amino acid side chains in restricted spaces can provide

159 ionalities that account for >50 mol % of the amino acid side chains in surface-priming Mfps-were show

160 The role of ionizable amino acid side chains in the bovine rhodopsin activatio

161 shown its function to be independent of the amino acid side chains in the contact region.

162 experimental data using water molecules and amino acid side chains in the distal pocket of the high-

163 as a model system to investigate the role of amino acid side chains in the formation of such fibrils.

164 arities, the positions of water molecule and amino acid side chains in the immediate Schiff base vici

165 in the loop connecting helices 11 and 12 and amino acid side chains in the pocket, which, together, e

166 ion to force solvent exposure of hydrophobic amino acid side chains in the regions flanking the helix

167 ted the disposition of several key catalytic amino acid side chains in the small subunit active site.

168 included the hydroxylation at C beta of two amino acid side chains in the vicinity of the cofactor,

169 he bridging water molecule and several other amino acid side chains in the vicinity of the ferroxidas

170 Because of the lack of information on the amino acid side chains in the x-ray structural model and

171 a place limits on the role of any single MHC amino acid side-chain in driving TCR binding in a peptid

172 etermine the relative importance of specific amino acid side-chains in defining the stability and fun

173 The accessible surface areas of amino acid side-chains in folded proteins are moderately

174 native and non-native interactions involving amino acid side-chains in these helices.

175 mCl, to identify potential interactions with amino-acid side chains in a nondenatured polypeptide sur

176 approach to estimate the surface exposure of amino-acid side-chains in the variable region directly f

177 ies using acetate as a model for carboxylate amino acid side chains indicate the nature of the coordi

178 in which the DNA is nearly straight, with no amino acid side chains inserted into the duplex, and the

179 netrate the membrane interface with aromatic amino acid side chains inserted into the hydrocarbon and

180 iate waters and in interfering with water or amino acid side chain interactions with DNA.

181 ed with an initial assessment of the citrate-amino acid side-chain interactions that may occur at the

182 consists of constructing a backbone and then amino acid side chains into an electron density map.

183 Furthermore, larger amino acid side chains introduced at gamma(2)A79 cause c

184 Those amino acid side chains involved in binding the dTDP-suga

185 These findings help elucidate the amino acid side chains involved in DNA binding and catal

186 Amino acid side chains involved in hydrogen bonds and el

187 As a means to evaluate the details of amino acid side chain involvement in substrate interacti

188 oborato-phosphonium salts supported by the L-amino acid side chain is described.

189 s indicate that the presence of a lipophilic amino acid side chain is fundamental to achieve good pot

190 reas the enzymatic activity is reduced, this amino acid side chain is not absolutely essential for ca

191 f the amide bond between the phenyl ring and amino acid side chain is prevented by a CH(2) bridge wer

192 ern of hydropathic states of protein surface amino acid side chains is invoked as the influence on th

193 These alterations of amino-acid side chains lead to higher structural and fun

194 CPT by altering the sizes and charges of key amino acid side chains, limiting accessibility of the ca

195 he anchor on the plasma membrane that govern amino acid side-chain-lipid interactions.

196 ce is mediated in part by contact between an amino acid side-chain located near the extreme C-terminu

197 -stabilizing interactions involving aromatic amino acid side chains make significant contributions to

198 ptide at the mMC4R, demonstrating that these amino acid side chains may be substituted for the imidaz

199 perturbations caused by chiral inversions of amino acid side-chains may be especially valuable in elu

200 transient pores and the insertion of charged amino acid side chains, may be common and perhaps centra

201 ydrophobicity scale") for the twenty natural amino acid side chains measured in the context of a nati

202 Aromatic amino acid side chains mediate most coat-internal scaffo

203 ptide isosteres have been employed to orient amino acid side chains mimicking the gauche(-) conformat

204 sults provide a specific illustration of how amino acid side chain mobility and burial or release con

205 4 A, on the order of the size of one to two amino acid side chains, much smaller than the FF domain

206 Interactions that involve one or more amino acid side chains near the ends of protein helices

207 tein-lipid interactions, primarily involving amino acid side chains near the membrane-water interface

208 The oxidation of amino acid side chains occurs at rates in accord with th

209 , with no significant contributions from any amino acid side chain of the proteins.

210 reviated as PTM, refers to the change of the amino acid side chains of a protein after its biosynthes

211 formation about the solvent accessibility of amino acid side chains of a protein.

212 omycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to

213 s of the naturally occurring i, i + 4, i + 7 amino acid side chains of an alpha-helix.

214 well established that even small changes in amino acid side chains of antigenic peptide bound to maj

215 ecifically, the Trp243 residue positions the amino acid side chains of Arg161 and Glu127 in specific

216 These results suggest that the amino acid side chains of flanking residues influence th

217 This study identifies those amino acid side chains of IL-22 that are individually im

218 lock protein synthesis by competing with the amino acid side chains of incoming aminoacyl-tRNAs for b

219 the formation of hydrogen bonds that involve amino acid side chains of residues in domains 1 and 2.

220 ric alpha-helical conformations exposing the amino acid side chains of the antibody binding sites.

221 ve work has focused on the importance of the amino acid side chains of the protein ligand, the role o

222 r an equatorial site for coordination to the amino acid side chains of the protein.

223 e generated in the presence of electron-rich amino acid side chains of the sort that may be present i

224 e solution were utilized to oxidize specific amino acid side chains of two model proteins (lysozyme,

225 The ACh-coordinating amino acid side-chains of the alpha subunits are far apa

226 r of four Mn ions and a Ca ion surrounded by amino acid side chains, of which seven provide ligands t

227 tion of a new carbon-carbon bond between two amino acid side chains on PqqA.

228 near the extreme C-terminus of SpoIVA and an amino acid side-chain on the hydrophilic face of the Spo

229 ievements employed methodologies that sample amino acid side-chains on a fixed backbone, while method

230 he outer forespore membrane via hydrophobic, amino acid side-chains on the hydrophobic face of the he

231 rent chemical probes (specifically different amino acid side chains or monovalent inorganic ions).

232 ced solely on the question of how changes in amino acid side-chain orientation, and the resultant alt

233 Quantitation of the amino acid side chain oxidation products generated by sy

234 n force (PMF) between all possible ionizable amino acid side chain pairs in various protonation state

235 ecursor ion as well as the presence of basic amino acid side chains, phosphate transfer reactions dur

236 t electrostatic interactions between charged amino acid side chains play an important role in determi

237 This work demonstrates that amino acid side chains play important roles in determini

238 This brings the total of amino acid side-chain positions that can be simultaneous

239 By changing the charge of amino acid side chains, posttranslational modification b

240 ractions between specific sugar moieties and amino acid side chains potentially important to the gp12

241 ype backbone fragment ions regardless of the amino acid side chains present in the parent bioconjugat

242 yrosines, contrary to suggestions that these amino acid side chains prevent tyrosine nitration.

243 At this resolution, most of the amino acid side chains produce recognizable density.

244 ch results in the active site recruitment of amino acid side chains proposed to play key roles in the

245 ivity results in oxidation at a multitude of amino acid side chains providing greater structural info

246 s of hydrogen bonds involving phosphorylated amino acid side chains (pSer, pAsp) with several common

247 3)H]dFBr is a photoaffinity probe with broad amino acid side chain reactivity.

248 uperfamily and contains all of the necessary amino acid side chains required for the hydrolysis of gl

249 and found excellent correlation between the amino-acid side chains required for in vitro assembly an

250 rce, because of a lack of negatively charged amino acid side-chain residues that would enable efficie

251 Amino acid side chains responsible for anchoring the sug

252 g the rotameric conformation adopted by some amino-acid side chains (rotamers) and resolving ordered

253 Changing the polar character of a single amino acid side chain (Ser-228) to a nonpolar residue tu

254 approach but also provide a way to quantify amino acid side chain-side chain interactions relevant t

255 Basic amino acid side chains situated in active sites may medi

256 The loss of amino acid side chains (small neutral losses, SNLs) from

257 ent rate of stable product formation of each amino acid side chain, so that the rate of oxidation of

258 bstitution, methylation at position 5 of the amino acid side chain (such analogues have not been prev

259 These data suggest that helix 6 contains amino acid side chains that are critical for transport a

260 te-specific installation of caging groups on amino acid side chains that are essential for protein fu

261 y mutagenesis to identify positively charged amino acid side chains that attract cytoplasmic Cl(-) io

262 ne, and in some instances, they also present amino acid side chains that interfere with binding.

263 mputational design techniques to select five amino acid side chains that play an important role in th

264 Scaffold 1 presents amino acid side-chains that are quite separated from eac

265 5 element, we searched this part of MelR for amino acid side-chains that might be able to interact wi

266 , such as 0.1 A, which ensures that for each amino-acid side chain the set contains a conformation wi

267 g specificity for the chemical nature of the amino acid side chain, the few peptides where this modif

268 ication strategy targeting an under-utilized amino acid side chain, this method provides convenient a

269 on geometry in biomolecules by reorientating amino acid side chains through substitution of L- to D-a

270 tably, the relative contributions of a given amino acid side chain to RNA polymerase inhibition and a

271 tate complex, (2) hydrogen transfer from the amino acid side chain to the indole chromophore, and (3)

272 us to manipulate the spatial orientation of amino acid side chains to alter the sterics of metal bin

273 ites of protonation, allowing all titratable amino acid side chains to be probed sequence specificall

274 l algorithm based on conserved properties of amino acid side chains to identify regions of known alle

275 the contributions of individual interfacial amino acid side chains to protomer-protomer affinity in

276 This alternation allows the amino acid side chains to segregate on opposite sides of

277 structure showed direct coordination of two amino acid side chains to the Fe(III) center (orange, se

278 The effects of hydrogen bonding of amino acid side chains to the nitrile probe are consider

279 esemblance of semirigid scaffolds expressing amino acid side-chains to PPI-interface regions could gu

280 be produced by elongating charge-containing amino-acid side chains to position the charges distally

281 These complexes illustrate how conserved amino acid side-chains, together with essential structur

282 of two interacting proteins in the format of amino acid side chains via the expansion of the genetic

283 s driven by a hydrophobic surface comprising amino acid side chains W287 and L290 located on the same

284 A reactivity order of amino acid side chains was obtained as Cys > Met > Trp >

285 t relies on cell-surface display of reactive amino acid side-chains was used to identify a diverse se

286 tributions from the peptide backbone and the amino acid side chains were calculated.

287 The reactivities of amino acid side chains were compared based on their loss

288 Alternative conformations for amino acid side chains were identified for 50 of the 748

289 y rearrangements in the orientation of local amino acid side chains which may be responsible for seal

290 -oxo-dG through allosteric interactions from amino acid side chains, which limit the anti-conformatio

291 We conclude that specific groupings of amino acid side-chains, which can be predicted from the

292 ypically focused on the reactivity of single amino acid side chains while ignoring the potential impo

293 components enables ready incorporation of an amino acid side chain with correct regio- and stereochem

294 The interactions of the amino acid side chains with a hydrophobic pocket near R4

295 gest a profound change in the orientation of amino acid side chains with the I-->M mutation.

296 n be rationalized by the interactions of the amino acid side chains with the substrate and the orient

297 nt for tightly interdigitating complementary amino acid side chains within specific domains of adjace

298 Amino acid side chains within the C-terminal domain of u

299 Rearrangements of particular amino acid side chains within the substrate channel and

300 Repositioning of amino acid side-chains without wholesale structural alte