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1 ports a key role for each residue within the peptide chain.
2  preserve the recognized conformation of the peptide chain.
3 s containing a thioamide bond in the nascent peptide chain.
4 f two loops connected by a flexible U-shaped peptide chain.
5  galectin that also has two CRDs in a single peptide chain.
6 en tyrosine was located in the middle of the peptide chain.
7 tion of the glycosyl amino acid units into a peptide chain.
8  incorporated at any desired position of the peptide chain.
9 ranslation and the rate of elongation of the peptide chain.
10 pecific residue position requirements in the peptide chain.
11 s, so different amino acids are added to the peptide chain.
12 e in the penultimate position of the nascent peptide chain.
13  interacting with the peptides to modify the peptide chain.
14 irectly couple thioimidates onto the growing peptide chain.
15  epimerization of stereogenic centers in the peptide chain.
16 slocase requirement for translocation of the peptide chain.
17 ipid chain and a coumarin fluorophore in the peptide chain.
18 s only a small degree of variation along the peptide chain.
19 Leu] at a single, unique, position along the peptide chain.
20 reaction between two terminal olefins on the peptide chain.
21 orporation of an amino acid into the growing peptide chain.
22 ll elongation at specific sites within their peptide chain.
23 trands that are cross-linked through pendant peptide chains.
24 integrity depends on the intertwining of two peptide chains.
25 ength, suggesting a lateral packing of three peptide chains.
26 ry structure consisting of two dimerized Rne-peptide chains.
27 n atoms with hydroxyl groups and cleavage of peptide chains.
28 onserved and primary modification of nascent peptide chains.
29 tif with a one-amino-acid offset between the peptide chains.
30 anonical offset of four residues between the peptide chains.
31 so affect fibrillogenesis and folding of the peptide chains.
32  a bundle of k adhering parallel polyglycine peptide chains.
33 to involve residues His-6 and His-14 of both peptide chains.
34 brils by reducing repulsions between amyloid peptide chains.
35  causes cotranslational scission of emerging peptide chains.
36 ed by processive enzymes and cross-linked by peptide chains.
37 ctional groups at the N-termini of poly-beta-peptide chains.
38                                 Two distinct peptide chains (A and B) were synthesized to model a sit
39 regation number is varied between k = 2 (two peptide chains adhering to each other with plenty of wat
40 eta(1-42) peptide chain to mitigate on-resin peptide chain aggregation, a presumed major source of sy
41 roup and the energy required to fragment the peptide chain allows the O-GlcNAc group to be detected a
42 proteins by ligating labelled and unlabelled peptide chains allows one to filter out unwanted informa
43  homogeneous NMP solutions by elongating the peptide chain alone the N-terminus.
44                    The combination of a long peptide chain along with the chromophore unit of PVD gen
45 ant calprotectin, consisting of 2 individual peptide chains also called migration inhibitory factor-r
46 he number of amino acid residues in the main peptide chain; amino acid residues attached to sulfur ar
47 Players were presented with a fully extended peptide chain and challenged to craft a folded protein s
48  a single lysine residue in an 11-amino acid peptide chain and human insulin.
49 cting domain pairs that are part of the same peptide chain and thus have an inter-domain peptide regi
50 (RF) to hydrolyze the ester bond between the peptide chain and tRNA.
51 a-amino acid can be controlled by the chiral peptide chain, and at the beta-position by using chiral
52 ar to assist in the expulsion of the growing peptide chain, and clamps at the ends of the mRNA tunnel
53  double-Gly(24)/Met(27) substitutions in the peptide chain, and compare their performance in GRPR-pos
54 ed by its application to the ligation of two peptide chains, and the generation of peptides with seve
55 ulky leucine side chain at position 3 in the peptide chain appears to play a role in the conformation
56                                     When the peptide chains are attached to the two different termini
57 m in which the C-terminally located DeltaPol peptide chains are cleaved intermolecularly to release t
58 ted with polysomes and the newly synthesized peptide chains are closely associated with molecular cha
59                And finally, the cross-linked peptide chains are dissociated from each other, and each
60                           To this end, Abeta peptide chains are functionalized with fluorescent tags,
61        Amyloids, fibrillar assembly of (poly)peptide chains, are associated with neurodegenerative il
62  targeting protein interfaces by extending a peptide chain around a non-canonical amino acid residue
63 (MeDbz) moiety that enables in a more robust peptide chain assembly.
64 ril polymorph to the distinctive dynamics of peptide chain association to their tips.
65 he rare cognate amino acids into the growing peptide chain at a rate of ~20 aa/s.
66 be removed, allowing the prolongation of the peptide chain at the C-terminus.
67 eries of coordination cages that incorporate peptide chains at their vertices, prepared through subco
68 ces between the unfolded states of even long peptide chains, at variance with expectations based on a
69 cients proved to be nearly uniform along the peptide chain, averaging to D = 0.49-0.55 x 10(-6) cm(2)
70 xceedingly complex process in which incoming peptide chains bind to the fibril while concertedly fold
71 n (grp) 170, have shown them to be efficient peptide chain-binding proteins.
72 ystallographically independent copies of the peptide chain, both at the receptor-binding site and els
73 nal modifications included elongation of the peptide chain by three residues at the N-terminus, its a
74 ndered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-alpha-aminoa
75 iological activity without preorganizing the peptide chains by covalent linkages.
76 pha-inhibitor (IalphaI, containing one light peptide chain called bikunin and two heavy chains) and p
77                                              Peptide chains can be cleaved selectively on the N-termi
78 cted determinants, most likely by creating a peptide chain cleavage in the antigenic molecule.
79                      Further assembly of the peptide chain, cleavage from the resin using 2-5% TFA in
80 riazene linkage, on-resin cyclization of the peptide chain, cleavage of the cyclic peptide from the r
81  used gelatin as the model protein since the peptide chains contain numerous sites capable of forming
82                   Synthesis of a 119-residue peptide chain containing 10 residues of the reverse tran
83 ides provides a novel strategy for accessing peptide chains containing unnatural vinyl glycine amino
84 abase contains over 5000 representative poly-peptide chains, covering all known structures in the PDB
85 es, indicators for N-terminal, C-terminal or peptide chain cross-link modifications, keywords, litera
86 luding amino-terminal, carboxyl-terminal and peptide chain cross-link modifications.
87 cations including N-terminal, C-terminal and peptide chain cross-link modifications.
88 ies; indicators forN-terminal, C-terminal or peptide chain cross-link modifications; keywords; and li
89 A is a D,d-endopeptidase able to cleave most peptide chain cross-links in V. cholerae's PG.
90 ete 180 degrees turn in the direction of the peptide chain define a reverse turn, a common motif and
91 lete 180 degree-turn in the direction of the peptide chain, define the beta-turn.
92 -like conformation with two loosely extended peptide chains, demonstrating the preference of the sequ
93 ncomycin was mapped to the N-terminus of the peptide chain, distinct from the binding site for Lipid
94 r a general hydrophobic collapse of the poly peptide chain driven by the change in solvent conditions
95 the stem plays an important role in securing peptide chains during translocation.
96                                              Peptide chain elongation as measured by polymerization o
97      Anti-EF-Tu antibodies similarly inhibit peptide chain elongation by P. aeruginosa ribosomes in t
98 chanism and performing the first step in the peptide chain elongation cycle.
99                        The machine is rapid: Peptide chain elongation is complete in hours.
100 lows characterization of both initiation and peptide chain elongation kinetics for cap-dependent tran
101  Two independent methodologies show that the peptide chain elongation rate increases as a function of
102      Temperature shift experiments show that peptide chain elongation rate increases immediately, whi
103 nd that a painful cue triggers repression of peptide chain elongation through activation of elongatio
104 tidyl transferase activity, a key enzyme for peptide chain elongation, was also significantly decreas
105 protein synthesis by controlling the rate of peptide chain elongation.
106 n to inhibit protein translation by reducing peptide chain elongation.
107 ther mobilized ER-associated Ca2+ nor slowed peptide chain elongation.
108 and they all showed reduced in vivo rates of peptide-chain elongation and increased levels of precurs
109                                              Peptide-chain elongation during protein synthesis entail
110 s associated with stimulation of the rate of peptide-chain elongation.
111 g" markedly increased the conductance of the peptide chain, especially when its location in the seque
112 L-Ala/D-Ala replacement in the middle of the peptide chain exhibited much higher diastereomeric resol
113 nd GTP as the essential energy ingredient in peptide chain extension all appeared from our laboratory
114 on by light of the diastereoselectivity of a peptide chain extension reaction.
115 ame on tmRNA that tags the defective nascent peptide chain for degradation.
116 y, partially unfolded state where one of the peptide chains forms a solvent-exposed loop.
117 cle into the growing polyketide/nonribosomal peptide chain from the precursors malonyl-CoA and cystei
118       The force-induced desorption of single peptide chains from mixed OH/CH(3)-terminated self-assem
119 sidues at positions 1 and 4, produced during peptide chain growth from L-Phe residues by 50 kDa epime
120  acidic, heat-stable sialoglycopeptide whose peptide chain has 100% homology to the putative sixth tr
121 lidine-type pseudoprolines (CF3-PsiPro) into peptide chains have been studied.
122 a disordered micellelike collection of a few peptide chains held together loosely by hydrophobic inte
123 raction by increasing the flexibility of the peptide chain; hence, the transition state would be dest
124 or incorporating multidentate ligands onto a peptide chain in a site-specific fashion.
125  phase, amino acids are added to the nascent peptide chain in accordance with codon sequences in the
126 its entropic destabilization relative to the peptide chain in isolation.
127 ld statherin, starting from a fully extended peptide chain in solution, in the presence of hydroxyapa
128  C terminus may result in the bending of the peptide chain in such a way that these two peptides come
129 etween the stalling of the elongated nascent peptide chain in the ribosome and its insertion through
130 ciculin reducing the segmental motion of the peptide chain in this local region.
131 tes, fast internal dynamics characterize the peptide chains in a way that is reminiscent of condensed
132 nced digestibility, characterized by shorter peptide chains in the digesta.
133 is contained on the top of a single stack of peptide chains in the fibril structure.
134 dicating a parallel alignment of neighboring peptide chains in the predominantly beta-sheet structure
135 ecause of a single amino acid offset between peptide chains in the triple helix, distinct heterotrime
136              Here, the method is extended to peptide chains in vacuum.
137 ine residues at specific locations along the peptide chain, in both the C-terminal and N-terminal dom
138 wn to play important roles in the eukaryotic peptide chain initiation process.
139 ing amino acid sufficiency to the control of peptide chain initiation.
140 er of mRNA species, the incorporation of the peptide chain into microsomes, and the topology of the p
141 cifically hydroxylates proline residues in a peptide chain into R-4-hydroxyproline, which is essentia
142 ly involves physical partitioning of nascent peptide chains into the lipid bilayer.
143  meso-diaminopimelic acid present in the PGN peptide chain is frequently observed.
144 tain friction forces as a single polyglycine peptide chain is pulled out of a bundle of k adhering pa
145 ferase AfcL and coenzyme A, the growing acyl-peptide chain is shuffled between different thioester ca
146  a disulfide bond near the middle of a short peptide chain is sufficient to nucleate some antiparalle
147 n is carried out in solution and the growing peptide chain is supported on a soluble tag, which confe
148 nformational transformation of each captured peptide chain is templated by the previously arrived pep
149  of as an alpha-carbon representation of the peptide chain, is a caricature of the sequence designed
150 am positive bacterial PG and degrades the PG peptide chains, leading to cell death.
151  different structural designs with different peptide chain length are chosen to construct two biosens
152 esidue glycine, to investigate the effect of peptide chain length on the appearance of macrocycle fra
153  specific amino acids nor a specific nascent peptide chain length was required for AAP to inhibit PTC
154 ediate, k(2), shows a dramatic dependence on peptide chain length, the rate constant for the intermed
155 and extrinsic physicochemical factors (e.g., peptide chain length, truncation, peptide concentration,
156 e amino acid assembly, resulting in variable peptide chain lengths.
157 ukin 5 (wt IL5) is composed of two identical peptide chains linked by disulfide bonds.
158 ose that Reh1 is displaced by the elongating peptide chain, making it the last assembly factor releas
159 annel, we propose that cleavage of the IP3 R peptide chain may alter other important regulatory event
160 tation have been investigated in an isolated peptide chain model (N-acetylphenylalaninylamide, NAPA)
161          Maintaining the fidelity of nascent peptide chain (NP) synthesis is essential for proteome i
162                     The incorporation into a peptide chain of highly hindered and weakly nucleophilic
163 yclic depsipeptide in contrast to the linear peptide chain of P39167-I and PA225-I.
164                                 Finally, the peptide chain of the resulting support-bound S-linked gl
165  friction forces for the relative sliding of peptide chains of Araneus diadematus spider silk within
166 cifically whether it can begin while nascent peptide chains of individual subunits are still attached
167 ndicates a preferred orientation between the peptide chains of the dimers.
168                          Both alpha and beta peptide chains of the human leukocyte antigen-DQ heterod
169 IFN-gamma SC1 was derived by linking the two peptide chains of the IFN-gamma dimer by a seven-residue
170 es show enhanced cell uptake over individual peptide chains of the same sequence, resulting in a sign
171 ons arises from the lack of hydration of the peptide chain on either side of the bulky aromatic side
172 tase has a limited capacity to translocate a peptide chain on its own.
173 ated with aqueous ammonia, which cleaved the peptide chain on the N-terminal side of cyanylated cyste
174 n(Mtt)-OH can be incorporated into a growing peptide chain on Wang resin.
175 eneral synthetic methods for the grafting of peptide chains onto polyoxometalate clusters by the use
176 nylation is the addition of prenyl groups to peptide chains or metabolites via the condensation of ge
177 d provide a model for controlled assembly of peptide chains or segments of larger proteins.
178 terns from single nanocrystals show that the peptide chains pack in parallel cross-beta columns with
179  the dimensions of beta-sheets with extended peptide chains perpendicular to the long axis of the agg
180          These data suggest that the growing peptide chain plays a role in modulating fluctuations be
181 resent at the adhesion sites) and k = 7 (one peptide chain pulled out from a close-packed cylindrical
182 mmunofluorescence microscopy or alpha 1 (IV) peptide chain quantitation by Western analysis and the a
183  We have determined the crystal structure of peptide chain release factor 1 (RF1) from Thermotoga mar
184 20480, that encode two predicted proteins, a peptide chain release factor 1 and a hemolysin acyltrans
185 2 into the 5' end of prfC, the gene encoding peptide chain release factor 3.
186 of of principle, we characterized eukaryotic peptide chain release factor subunit 3a (eRF3a/GSPT1), w
187 w that on partitioning into the bilayer, the peptide chains remain in contact with lipid headgroups.
188 ective MS/MS conditions, and the dissociated peptide chains remained intact during MS(2), thus enabli
189 passivation of other reactive handles on the peptide chain, representing the applicability of biocata
190 escent tag is cleaved off from the substrate peptide chain resulting in an approximately 100-fold inc
191                                The resulting peptide chain reveals that the activated phosphonium yli
192 tamyl)lysine cross-links, connecting various peptide chain segments, are frequently the major product
193   This study shows that folding is rapid and peptide chain self-cleavage occurs early for subunits ad
194               Nevertheless, thrombin cleaves peptide chains solely after Arg, and trypsin after Lys a
195 ed the minor structural changes in proteins (peptide chain structure, Amide I, Amide II, alpha-helix,
196 ssible steps take place at the center of the peptide chain; subsequently, several pathways appear to
197             The hydrophobic structure of the peptide chains suggests that they act as symmetric deter
198 d in several translational events, including peptide chain termination and decoding accuracy.
199 nucleotide 1054 are the result of defects in peptide chain termination rather than of decreases in ge
200 sion is limited by release factor-1-mediated peptide chain termination.
201  in one or more specific interactions during peptide chain termination.
202 cific interaction of the loop is involved in peptide chain termination.
203 ested by release of the mRNA by puromycin, a peptide chain terminator.
204 ode MALDI-ISD and found good coverage of the peptide chain termini starting from c'2 and z'2 fragment
205 tends beyond "simple" generation of a linear peptide chain that folds into a tertiary structure, pote
206  methionine sixth heme ligand and the nearby peptide chain that has been implicated in electron trans
207 tic molecular dynamics simulations for short peptide chains that are laterally pulled over planar hyd
208 ey involve the collective motions of several peptide chains that are not guided by a funneled energy
209                       Specifically, the four peptide chains that comprise the filter adopt an unusual
210                      Considering the unusual peptide chain, the elucidation of the structure presente
211 ydrogen bond to primary binding sites on the peptide chains, the enthalpy was approximately constant
212 lycan strands that are cross-linked by short peptide chains, the mature cell wall is chemically diver
213 istance between interacting atoms on vicinal peptide chains thereby increasing the electrostatic inte
214 erine, and alanine residues in the middle of peptide chains, thereby providing a biochemical capabili
215                      Attachment of a growing peptide chain to a glycylaminomethyl resin via a thiogly
216 ise solid-phase assembly of the A beta(1-42) peptide chain to mitigate on-resin peptide chain aggrega
217 the same steps as those of natural collagen (peptide chain to triple helix to nanofibres and, finally
218  of the TREN scaffold which allows the three peptide chains to adjust their register for a tighter tr
219                              The tendency of peptide chains to aggregate is translated into a list of
220 ons are performed on a system of eight model peptide chains to study how the competition between prot
221 e or more glutamic acid residues as branched peptide chains to the C-terminal tails of both alpha- an
222   Analysis of the heme group arrangement and peptide chain topology of RoxA confirmed a distant kinsh
223 w instrument for the direct manufacturing of peptide chains up to 164 amino acids long over 327 conse
224                    The remaining part of the peptide chain was modeled as a mixture of three sequence
225 iency by secondary structures of the nascent peptide chain, we performed a comparative analysis in ba
226                                 This growing peptide chain wends its way through the ribosomal tunnel
227            The extended conformations of the peptide chains were confirmed by 1D and 2D NMR.
228 tion, and Fourier transform IR suggested the peptide chains were in a parallel (AcVYK, AcPHF6) or ant
229 ovement of the helix/coil boundary along the peptide chain, which leads to slower unfolding kinetics
230 en bonds with the backbone of the subsequent peptide chain, while lysine and glutamine less frequentl
231 d distances in this core region of the Abeta peptide chain with solid-state NMR.
232 d radius 2.30+/-0.05 nm surrounded by 49+/-4 peptide chains with a partial specific volume of 0.7 cm3
233 -packed cylindrical array of six neighboring peptide chains with no water inside the bundle).
234 us coupling with amine groups of two growing peptide chains, with excellent yields (30-70%).
235 well defined composition and register of the peptide chains within the helix, based on information en
236 elf-solvated globule conformation, where the peptide chain wraps around and solvates the charge locat

 
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