ライフサイエンスコーパス: peptide bond

1 n a cis- or trans-configured Glu(18)-Pro(19) peptide bond.

2 e surrounding extein fragments with a native peptide bond.

3 rans isomerization of one particular proline peptide bond.

4 some takes place following formation of each peptide bond.

5 lanking polypeptides (exteins) with a native peptide bond.

6 age of glycosidic bonds without breaking the peptide bond.

7 pecifically stimulate formation of the first peptide bond.

8 modified to join the N and C termini with a peptide bond.

9 face, induced by distortions of the backbone peptide bond.

10 ahel peptides, indicating exclusion from the peptide bond.

11 em-diol intermediate and (2) cleavage of the peptide bond.

12 nsion and its characteristic cis-Ile54-Pro55 peptide bond.

13 orbital (pi*) of C(i)=O(i) of the subsequent peptide bond.

14 udy a reaction similar to the formation of a peptide bond.

15 calcium ions triggers the formation of a cis peptide bond.

16 th N-methylacetamide chosen to represent the peptide bond.

17 sed strain on the already weak His207-Arg208 peptide bond.

18 disrupted by a flip of the Glu(192)-Gly(193) peptide bond.

19 ing is coordinated by an unusual cis-Ala-Ala peptide bond.

20 ed 180 degrees rotation of the Met109-Gly110 peptide bond.

21 ed in the active site for resynthesis of the peptide bond.

22 carbonyl group (C(i)=O(i)) of the subsequent peptide bond.

23 es in which an oxirane replaces the scissile peptide bond.

24 of occurrence in fragmentation of the second peptide bond.

25 r a second gas phase mechanism at the second peptide bond.

26 located directly N-terminal to the scissile peptide bond.

27 should readily block the formation of every peptide bond.

28 APN degradation due to a distorted scissile peptide bond.

29 ein-succinimide product and scission of that peptide bond.

30 gamma-glutamyl amide linkages and/or unusual peptide bonds.

31 s isomerization of the N13-P14 and P100-P101 peptide bonds.

32 iles and hydroxybenzotriazole, gives rise to peptide bonds.

33 sequence motif that can stabilize Pro-cisPro peptide bonds.

34 o peptide bonds of tripeptides into selenoxo peptide bonds.

35 for the stabilization of two high-energy cis peptide bonds.

36 city to hydrolyze thioester, isopeptide, and peptide bonds.

37 relation between the cis/trans states of the peptide bonds.

38 forms allows for the selective formation of peptide bonds.

39 g the conformation of specific pSer/pThr-Pro peptide bonds.

40 erminal tail, and trans conformation for the peptide bonds.

41 fering from sequence-defined polymers having peptide bonds.

42 the cis-trans isomerization of Xaa(1)-Pro(2) peptide bonds.

43 y of the liposomes promotes the formation of peptide bonds.

44 the cis-trans isomerization of Xaa(1)-Pro(2) peptide bonds.

45 At the P-site, proline is slow in forming peptide bonds.

46 of conformational motion at or near specific peptide bonds.

47 t ovalbumin aggregation rendered a number of peptide bonds accessible to digestive proteases which we

48 l change of the isomeric state of the prolyl peptide bond acts as a switching mechanism in altering t

49 e oxidized state, an unusual non-proline cis-peptide bond adjacent to one of the cysteines introduces

50 thermally stable mutants, the L94(L)-S95(L) peptide bond adopts an energetically unfavorable non-X-p

51 d by factors XIa or VIIa, by cleavage of the peptide bonds after Arg145 and Arg180.

52 4 with residues that strongly prefer a trans peptide bond (Ala, Gly) results in significant populatio

53 Notably, the N448-P449 peptide bond also plays a critical role for the intercon

54 ring hydrogen-deuterium exchange patterns of peptide bond amide protons monitored by mass spectrometr

55 1,2,3]triazolyl moiety is isosteric with the peptide bond and can function as a surrogate of the clas

56 hich the disulfide A11-B10 was replaced by a peptide bond and found that cAMP production ceased while

57 PXTG-containing proteins at the scissile T-G peptide bond and ligates protein-LPXT to the terminal Gl

58 ols the orientation of the Glu(192)-Gly(193) peptide bond and the correct architecture of the oxyanio

59 age occurs most efficiently at the LN1036-37 peptide bond and to a lesser extent at three other sites

60 arboxylate metal ligand, a resulting twisted peptide bond, and the off-line geometry for dioxygen coo

61 mutations, cleaves human IL-23 at the target peptide bond, and when pre-mixed with IL-23 in primary c

62 sight into the formation of modern ribosomal peptide bonds, and a means for the emergence of peptides

63 iazole is a well-recognized bio-isostere for peptide bonds, and peptides with one or more triazole un

64 the hydrogen-bonding network around the cis-peptide bond are well conserved within the metallopeptid

65 the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which g

66 yze the isomerization of the phospho-Thr-Pro peptide bond at the turn motif, thus converting these PK

67 a condensation reaction selectively forming peptide bonds at the air-water interface.

68 Specific electrochemical cleavage of peptide bonds at the C-terminal side of tyrosine and try

69 in LSF permits isomerization by Pin1 of the peptide bonds at the nearby phosphorylated SP motifs (Se

70 mechanism by which the cleavage of multiple peptide bonds awaits the "almost complete" delivery of a

71 The reorganization also changes the peptide bond between Asp153, a ligand of the single zinc

72 talyses the formation of an irreversible iso-peptide bond between lysine 50 and glutamic acid 270 on

73 ss spectrometry showed that IpaJ cleaved the peptide bond between N-myristoylated glycine-2 and aspar

74 lyzes the formation of an intermolecular iso-peptide bond between residues E270 and K50 located in th

75 nd other enzymes that selectively cleave the peptide bond between the proline and the phenylalanine a

76 substrate, thus causing the rotation of the peptide bond between the two residues.

77 e and results in the formation of a covalent peptide bond between Urm1 and its substrates.

78 ative method was developed to form amide and peptide bonds between amines and primary nitroalkanes si

79 hat catalyzes the cis/trans isomerization of peptide bonds between proline and phosphorylated serine/

80 2,3-triazole moiety can be incorporated as a peptide bond bioisostere to provide protease resistance

81 Mouse chymotrypsin B also cleaved the same peptide bond but was 7-fold slower.

82 teolytic events: cleavage of the Leu81-Glu82 peptide bond by chymotrypsin C (CTRC) and cleavage of th

83 n C (CTRC) and cleavage of the Arg122-Val123 peptide bond by trypsin.

84 st peptides by proteolytic cleavage at Arg-X peptide bonds by arginine gingipains, followed by citrul

85 However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to

86 trifluoromethyl group, we show that the cis peptide bond can be readily switched from 0% to 100% in

87 ied: amino acid side chains can be modified, peptide bonds can be cleaved or isomerized, and disulfid

88 c VWF and FRETS-VWF73 at the V(1607)-T(1608) peptide bond; cathepsin G and matrix metalloprotease 9 c

89 t efficiently catalyzed citrulline-dependent peptide bond cleavage (kcat/KM = 6.9 x 10(5) M(-1)s(-1))

90 D) of the zn* fragments resulted in specific peptide bond cleavage adjacent to the binding site of 1,

91 d that provide insight into the chemistry of peptide bond cleavage and establish the role of Thr1 Oga

92 triads of fragmentation ions resulting from peptide bond cleavage and further neutral loss of either

93 rization of the ATP- versus AMPPNP-dependent peptide bond cleavage and the delivery of the scissile s

94 The kinetic profile of peptide bond cleavage at different regions of lambdaN wa

95 we propose a revised catalytic mechanism of peptide bond cleavage by DapE enzymes.

96 These results show that electrochemical peptide bond cleavage in a microfluidic cell is a novel,

97 h residue 1 being predominantly l-isoAsp and peptide bond cleavage next to Ser 8 is also evident.

98 t asparagine residues indicates that not all peptide bond cleavage occurs by hydrolysis.

99 ked to differences in enzyme selectivity for peptide bond cleavage of camel and bovine milk proteins

100 serves as the base in the first step of the peptide bond cleavage reaction.

101 l residues of oxidized trunc-TtRp have trans peptide bond configurations but that two of these peptid

102 ctra and the same pattern of peptidyl-prolyl peptide bond configurations by NMR, and both appear to b

103 The peptidyl-prolyl peptide bond configurations were determined by analyzing

104 he puckering of the oxazolidine ring and the peptide bond conformation.

105 nique ability to populate both cis and trans peptide bond conformations may allow proline to act as a

106 ermediates before accessing their cis prolyl peptide bond-containing native conformations.

107 leavage site in VWF, the Tyr(1605)-Met(1606) peptide bond, contains both oxidation-prone residues.

108 new ends through the cleavage of an existing peptide bond, CP can perturb local tertiary structure an

109 s a microbial toxin mechanism acting via iso-peptide bond cross-linking between host proteins and is,

110 de bond configurations but that two of these peptide bonds (Cys151-Pro152 and Gly169-Pro170 located n

111 e energy barrier to the formation of the cis peptide bond decreases from 21.4 kcal/mol in the absence

112 tions: peptidyl transfer, the formation of a peptide bond during protein synthesis, and peptidyl hydr

113 tRNA(i)(fMet) for the formation of the first peptide bond during translation initiation.

114 e locally there is much disorder, especially peptide bond flipping.

115 Cleavage of the peptide bond following electrochemical oxidation of Tyr

116 and the nascent peptide cooperate to inhibit peptide bond formation and induce translation arrest.

117 plex molecular machine, but the mechanism of peptide bond formation and the origin of the catalytic p

118 tRNA at the A-site, leading to inhibition of peptide bond formation and translation arrest.

119 explain how the rates of GTP hydrolysis and peptide bond formation are controlled by the mRNA codon

120 implest means of activating a thiol acid for peptide bond formation at neutral pH.

121 ng during translation correlates with slowed peptide bond formation at successive proline sequence po

122 report unambiguous spectroscopic evidence of peptide bond formation at the air-water interface, yield

123 s of faithfully decoding mRNA and catalyzing peptide bond formation at the peptidyl transferase cente

124 a specific requirement for eIF5A to promote peptide bond formation between consecutive Pro residues.

125 lide action involves selective inhibition of peptide bond formation between specific combinations of

126 ghter-binding aa-tRNAs show reduced rates of peptide bond formation due to slow release from EF-Tu*GD

127 ondensation domain, which typically performs peptide bond formation during product assembly, also syn

128 In this scenario, peptide bond formation emerged to drive unidirectional m

129 er than the uncatalyzed rate of nonribosomal peptide bond formation from activated amino acids.

130 g of their CCA-ends into the PTC thus making peptide bond formation impossible.

131 that similar mechanisms are involved in the peptide bond formation in aqueous solution and in the ri

132 ructures have shown that the active site for peptide bond formation is composed entirely of RNA.

133 delivery to the ribosome by EF-Tu, not slow peptide bond formation on the ribosome.

134 required for irreversible GTP hydrolysis and peptide bond formation plays a key role in the fidelity

135 In this paper we present a study of the peptide bond formation reaction catalyzed by ribosome.

136 y of correct aminoacyl-tRNA to the ribosome, peptide bond formation results in a rapid conformational

137 nti-IgG antibodies were then coupled through peptide bond formation to acidic functional groups on th

138 abrogate the ability of the PTC to catalyze peptide bond formation with a particular subset of amino

139 The peptide bond formation with the amino acid proline (Pro)

140 as dictated by the mRNA codon, catalysis of peptide bond formation, and movement of the tRNAs and mR

141 ted cycles of the binding of aminoacyl-tRNA, peptide bond formation, and translocation.

142 Here we report the transition state of peptide bond formation, based on analysis of the kinetic

143 ingly, the key chemical step of translation, peptide bond formation, is among the slower enzymatic re

144 chemical step of natural protein synthesis, peptide bond formation, is catalysed by the large subuni

145 mical reactivity hypothesis and arguing that peptide bond formation, not accommodation, is rate limit

146 ssesses all of the capabilities required for peptide bond formation, seems to be still functioning in

147 cid substrates influence the fundamentals of peptide bond formation.

148 by release factors and, to a lesser extent, peptide bond formation.

149 e Met-puromycin synthesis, a model assay for peptide bond formation.

150 inding of an A-site tRNA, thereby inhibiting peptide bond formation.

151 The SRL also is not essential for peptide bond formation.

152 providing a framework for directed covalent peptide bond formation.

153 its the ribosome prior to the first cycle of peptide bond formation.

154 alyzed GTP hydrolysis and ribosome-catalyzed peptide bond formation.

155 s, and during wetting-drying cycles, promote peptide bond formation.

156 ne, deciphers the genetic code and catalyzes peptide bond formation.

157 ome for the next round of tRNA selection and peptide bond formation.

158 into the aminoacyl (A) site, operate before peptide bond formation.

159 e and versatile tool for the ring closure by peptide bond formation.

160 in, and a condensation domain that catalyzes peptide bond formation.

161 ation of tRNA and mRNA on the ribosome after peptide bond formation.

162 odation intermediates and thereby inhibiting peptide bond formation.

163 thodology provides an alternative method for peptide bond formation.

164 been widely explored in the selective amide/peptide bond formation.

165 lated tRNA is established spontaneously upon peptide bond formation; this event involves coupled move

166 gation factor P (EF-P), which by stimulating peptide-bond formation allows translation to resume.

167 showed no defects in mRNA and tRNA binding, peptide-bond formation and sparsomycin-dependent translo

168 One example is SecM, which inhibits peptide-bond formation in the ribosome's peptidyl transf

169 effectors of messenger RNA (mRNA) decoding, peptide-bond formation, and ribosome dynamics during tra

170 ng fundamental insight into the mechanism of peptide-bond formation, our findings suggest how the seq

171 cid proline is a poor donor and acceptor for peptide-bond formation, such that translational stalling

172 he elimination of a water molecule for every peptide bond formed, and are thus unfavorable in aqueous

173 cts the carrier domain cofactor bound to the peptide bond-forming condensation domain, whereas a seco

174 hus represents a new group of tRNA-dependent peptide bond-forming enzymes in secondary metabolite bio

175 The peptide-bond-forming catalyst region can be removed from

176 uoromethyl group in the stabilization of the peptide bond geometry.

177 highly strained conformation at the scissile peptide bond, had been identified and was hypothesized t

178 f peptide fragments using a dynamic covalent peptide bond has not yet been achieved without enzymatic

179 Many high-yielding reactions for forming peptide bonds have been developed but these are complex,

180 Approximately 70% of assessable peptide bond hydrogens were protected from exchange suff

181 ing was relatively weak or for a majority of peptide bond hydrogens.

182 Aminopeptidases catalyze N-terminal peptide bond hydrolysis and occupy many diverse roles ac

183 V(L) domains catalyze peptide bond hydrolysis independent of V(H) domains.

184 and processivity may be achieved by coupling peptide bond hydrolysis to the binding and release of su

185 , quantifying the extent of racemization and peptide bond hydrolysis using reverse-phase high-perform

186 alternating between epoxide ring opening and peptide bond hydrolysis, assisted by E271 and E296, resp

187 chemical environment in the GPS to catalyse peptide bond hydrolysis.

188 hains (VL and VH domains) of Ig can catalyze peptide bond hydrolysis.

189 We report the superior amide and peptide bond-hydrolyzing activity of the same heavy and

190 Peptide bond-hydrolyzing catalytic antibodies (catabodie

191 glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated resi

192 glutamate binding causes an aspartate-serine peptide bond in a flexible part of lobe 2 to rotate 180

193 bonyl oxygen on the N-terminal of the prolyl peptide bond in a predominately unidirectional fashion.

194 Reduction of the Lys-Dmt peptide bond in cyclodal resulted in an analogue, c[-d-A

195 t cis-trans isomerization of the Ile88-Pro89 peptide bond in cytochrome P450(cam) (CYP101).

196 cis-trans isomerization of the proline imide peptide bond in many cell signaling pathways.

197 n that stimulates the formation of the first peptide bond in protein synthesis.

198 mediated cleavage of the Tyr(1605)-Met(1606) peptide bond in the A2 domain.

199 ed by the state of isomerization of a prolyl peptide bond in the active site.

200 use Ctrc readily cleaved the Phe-150-Gly-151 peptide bond in the autolysis loop of T8 and T9 and inhi

201 nvolved slow cleavage of the Leu-149-Ser-150 peptide bond in the autolysis loop.

202 active site of Ssu72, with the pSer 5-Pro 6 peptide bond in the cis configuration, which contrasts w

203 trate the lack of recognition of the central peptide bond in the dipeptide, potentially enabling the

204 iated by the cleavage of the Arg(13)-Gln(14) peptide bond in the loop region, a catastrophic proteoly

205 roteolytic cleavage of the Arg(494)-Val(495) peptide bond in the zymogen-like pro-HGF results in allo

206 Moreover, peptide bond in tripeptides formed more tri-HAcAms than

207 prolyl isomerization of the Asp(29)-Pro(30) peptide bond in wild-type AHSP because it was absent whe

208 of cis-trans isomerization of the two prolyl-peptide bonds in BK[1-5](2+).

209 -2, and it readily cleaved the reactive-site peptide bonds in eglin C and ecotin.

210 ng the backbone connectivity by breaking all peptide bonds in lysozyme, we find that the hysteresis s

211 phosphate groups and the Pi electrons of the peptide bonds in PNA.

212 cis peptide bonds in proteins are often rate-limiting steps

213 Furthermore, we show that those peptide bonds in proteins that are most nonplanar, devia

214 fusion protein substrates position alternate peptide bonds in register with the antibody catalytic su

215 Proteases enzymatically hydrolyze peptide bonds in substrate proteins, resulting in a wide

216 avage of two disulfide bonds and up to three peptide bonds in the kringle 5 domain of the protein.

217 conformations for both the first and second peptide bonds in the monomers, and a two-dimensional che

218 o be determined by the fraction of cis X-Pro peptide bonds in this region.

219 Due to the presence of peptide bonds in tripeptides, Tyr-Tyr-Tyr and Ala-Ala-Al

220 with implications on the role played by cis-peptide bonds in unfolded proteins.

221 line-I helix (PPI, having all cis-configured peptide bonds) into polyproline-II (PPII, all trans) hel

222 The Tyr-Gln peptide bond inversion appears to involve a progressive

223 osecond timescale but does not reproduce the peptide bond inversion between loop residues Tyr269 and

224 ith the substrate, and creation of a twisted peptide bond involving this carboxylate and the followin

225 icing pathway in which the upstream scissile peptide bond is consecutively rearranged into two thioes

226 and transfer RNA on the ribosome after each peptide bond is formed, a process termed translocation.

227 As and messenger RNA by one codon after each peptide bond is formed, a reaction that requires ribosom

228 when a second aminoacyl-tRNA is bound and a peptide bond is formed.

229 of H3 at the alanine 15-proline 16 (A15-P16) peptide bond is influenced by lysine 14 (K14) and contro

230 The Leu81-Glu82 peptide bond is located within a calcium binding loop, a

231 Cleavage of peptide bonds is a major mechanism of protein control in

232 Formation of l-isoaspartyl (isoAsp) peptide bonds is a major source of protein damage in viv

233 The planarity of peptide bonds is an assumption that underlies decades of

234 s, so the cis/trans isomerization of proline peptide bonds is the rate-limiting step during triple-he

235 l Ibeta-strand and an accompanying N448-P449 peptide bond isomerization in the preceding HI loop.

236 Therefore, the peptide bond may be an important indicator to predict th

237 o Pro-tRNA(Pro), productive synthesis of the peptide bond occurs.

238 tein excision and rearrangement into the new peptide bond occurs.

239 ed cells, indicating that the NH(2)-terminal peptide bond of Asp(452) is essential for the initiation

240 Here we demonstrate that the Leu81-Glu82 peptide bond of human cationic trypsin, but not trypsino

241 hia coli hydrolyzes the terminal D-Ala-D-Ala peptide bond of the stem peptides of the cell wall pepti

242 ced binding requires the N-end residue and a peptide bond of the substrate, as well as multiple aspec

243 nesis, including backbone mutagenesis of the peptide bond of the vicinal disulfide, we have establish

244 rsed in the solution containing trypsin, the peptide bonds of BSA were hydrolyzed and peptide fragmen

245 yze the interconversion of the cis and trans peptide bonds of prolines.

246 Because proteases irreversibly cleave peptide bonds of protein substrates, their activity must

247 enation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds

248 hat Fv-cmp is an endoprotease that cleaves a peptide bond on the C-terminal side of the lectin domain

249 IgG hydrolyzed peptide bonds on the C-terminal side of basic amino acid

250 ontaining triazole and the other with native peptide bonds, on a gold substrate was studied by quartz

251 is accomplished through the formation of two peptide bonds, one between an amine-terminated PEG and t

252 imited to stimulating synthesis of the first peptide bond or that eIF5A functioned on only a subset o

253 e lone pairs (n) of the oxygen (O(i-1)) of a peptide bond over the antibonding orbital (pi*) of C(i)=

254 e lone pairs (n) of the oxygen (O(i-1)) of a peptide bond over the antibonding orbital (pi*) of the c

255 eference for C (gamma)- exo pucker and trans peptide bond, P4H appears to discriminate against the co

256 hat catalyzes cis-trans isomerization of the peptide bond preceding a proline and promotes folding an

257 cis) template possesses a characteristic cis peptide bond preceding Ala(5), which results in type VI

258 hat stabilizes the trans conformation of the peptide bond preceding hyp, endowing hyp with the unusua

259 ivity was highly specific and hydrolysed the peptide bond predominantly on the carboxy side of Glu re

260 the result of a previously unidentified cis-peptide bond present in the monomeric state.

261 o the active site, contains two adjacent cis-peptide bonds, Pro 386 and Tyr 387.

262 inus reveals a less stable His207-Arg208 cis peptide bond, providing a rationalization for its sponta

263 65%, while replacing disulfide A10-A15 by a peptide bond reduced binding affinity to 32% and lowered

264 ntrast, replacing the disulfide A24-B22 by a peptide bond reduced potency proportional to the binding

265 The carboxyl oxygen of an adjacent peptide bond serves as the sixth ligand that completes t

266 Peptide bonds strongly deviating from planarity are cons

267 ls cleave FRETS-VWF73 at the V(1607)-T(1608) peptide bond, suggesting that elastase or PR3 expressed

268 NAs embracing two amino acids with a linking peptide bond supports the idea that a direct-RNA-templat

269 Whereas ribosomes efficiently catalyze peptide bond synthesis by most amino acids, the imino ac

270 -puromycin synthesis-a model assay for first peptide bond synthesis thought to report on certain aspe

271 air-water interface as a favorable venue for peptide bond synthesis, and demonstrate the occurrence o

272 e site of 23S rRNA ribozyme, which catalyzes peptide bond synthesis, was both necessary and sufficien

273 loop in GR is an extreme case of sequential peptide bonds systematically deviating from planarity--a

274 ore, these mutant enzymes hydrolyze the same peptide bond that is recognized by the corresponding ful

275 It would be of interest to know whether peptide bonds that involve the nitrogen atoms of cystein

276 Moreover, the peptide bonds that were cleaved appeared to be specific

277 ed target sequence was evident, although the peptide bonds that were susceptible to proteolysis were

278 n indeed lead to proteolysis of the adjacent peptide bond, thereby providing substantive support for

279 the calcium ions not only stabilize the cis peptide bond thermodynamically but also catalyze its for

280 II activation peptide segment at the R37-G38 peptide bond, thrombin assists in activating the transgl

281 from the FAD cofactor acting to polarize the peptide bond through interaction with the carbonyl oxyge

282 he initial event in protein self-splicing, a peptide bond to the nitrogen atom of an internal cystein

283 ide sensor element attached by an N-terminal peptide bond to the trans mouth of the pore.

284 serine are more susceptible to cleavage than peptide bonds to amino acids that lack reactive side cha

285 been thought to drive the prolyl-containing peptide bonds to the trans configuration needed for trip

286 ssuming fixed bond lengths, bond angles, and peptide bond torsions, as well as ignoring molecular int

287 Due to its nature, the peptide bond undergoes a spontaneous cis-trans isomerism

288 rgy simulations of the formation of this cis peptide bond using a combined quantum mechanics/molecula

289 trans conformations about the central prolyl peptide bond was investigated by integration of signals

290 The thermodynamic stability of the scissile peptide bond was not dependent on CTRC or Leu-81, as re-

291 sin was incubated with CTRC, the Leu81-Glu82 peptide bond was re-synthesized to establish the same eq

292 Cleavage depended on ATP and the correct peptide bond was shown to be cleaved using a rapid and s

293 fferent cis/trans geometry at the key prolyl peptide bonds were designed, covering a promising confor

294 the kinetics of deuterium incorporation into peptide bonds were examined by mass spectrometry.

295 degrading Abeta(1-42), although the targeted peptide bonds were identical.

296 correct orientation of the Glu(192)-Gly(193) peptide bond, which is likely flipped in the absence of

297 FT-IR spectra confirmed the formation of new peptide bonds, which significantly improved stability of

298 rs, from building blocks linked by olefin or peptide bonds, with a sequence defined by a reconfigurab

299 Intramembrane proteases hydrolyze peptide bonds within the cell membrane as the decision-m

300 es RNA polymerase II (pol II) by isomerizing peptide bonds within the pol II carboxy-terminal domain