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1 -tryptophan variants encompassing the entire polypeptide chain.
2 ependent structural or functional units of a polypeptide chain.
3 space of folded structures accessible to the polypeptide chain.
4 ment that precedes the fusion peptide in the polypeptide chain.
5 ut because it forms a nanopore from a single polypeptide chain.
6 e efficiently performed by components of the polypeptide chain.
7 ously tested Shigella antigens into a single polypeptide chain.
8 nd thermodynamic consequences of threading a polypeptide chain.
9 related structures and includes the complete polypeptide chain.
10 Pasteurella heparosan synthases in a single polypeptide chain.
11 ing state or contain a defined translocating polypeptide chain.
12 s several distinct functions within a single polypeptide chain.
13 oglutamate can form on the N terminus of the polypeptide chain.
14 domain (DBD) occur multiple times within one polypeptide chain.
15 se domain, and a protease domain, all in one polypeptide chain.
16 ive molecular motion for the majority of the polypeptide chain.
17 are similar to those imposed on the nascent polypeptide chain.
18 ore with an unexpected crosslink to the main polypeptide chain.
19 increase the rigidity and compactness of the polypeptide chain.
20 mains present adjacent to each other along a polypeptide chain.
21 ching through different conformations of the polypeptide chain.
22 and transfers an Ala residue to the growing polypeptide chain.
23 chain connected by linkers to form a single polypeptide chain.
24 the characteristics of a completely unfolded polypeptide chain.
25 -ene and dioxygen) are derived from the same polypeptide chain.
26 hich we localize to specific segments of the polypeptide chain.
27 chanical transduction through titin's intact polypeptide chain.
28 structural and biophysical properties of the polypeptide chain.
29 ost always arranged sequentially in a single polypeptide chain.
30 omal RNA, and alters the path of the nascent polypeptide chain.
31 of an IgG1 and at multiple sites in the same polypeptide chain.
32 nce, but rather to the mature portion of the polypeptide chain.
33 llow the passive directional movement of the polypeptide chain.
34 multiple cellular functions within a single polypeptide chain.
35 ibosome exerts a destabilizing effect on the polypeptide chain.
36 n9GlcNAc2 oligosaccharides as well as to the polypeptide chain.
37 y a long intrinsically disordered N-terminal polypeptide chain.
38 tryptophan at different locations along the polypeptide chain.
39 ociated with the signal-transducing FcRgamma polypeptide chain.
40 wn function (DUF) near the C terminus of the polypeptide chain.
41 signal peptide produces N-terminal elongated polypeptide chains.
42 ng templates, such as properly folded DNA or polypeptide chains.
43 in to Levinthal's paradox for the folding of polypeptide chains.
44 ns seems to constitute a generic property of polypeptide chains.
45 ith the inherent aggregation propensities of polypeptide chains.
46 bunit is composed of one CL-L1 and two CL-K1 polypeptide chains.
47 the tight interleaving of their constituent polypeptide chains.
48 electrostatic interactions between adjacent polypeptide chains.
49 events premature degradation of such nascent polypeptide chains.
50 with the rate of formation differing between polypeptide chains.
51 ed with processes that involve misfolding of polypeptide chains.
52 ion of full-length, chemically denatured GFP polypeptide chains.
53 es that mediate the ATP-dependent folding of polypeptide chains.
54 ed with secondary structure formation of the polypeptide chains.
55 is to generate two non-covalently associated polypeptide chains.
56 mutual synergistic folding of two disordered polypeptide chains.
57 e ribosome through an exit tunnel as nascent polypeptide chains.
58 e of ribosomes and incorporates into nascent polypeptide chains.
59 ide bonds link pairs of cysteine residues in polypeptide chains.
60 e extended chains, hairpins, and crosslinked polypeptide chains.
61 ino acids away from the synthesis of nascent polypeptide chains.
62 increase of the number of GABs on individual polypeptide chains.
63 otein folding limits the lengths of cellular polypeptide chains.
64 t restrict the conformational freedom of the polypeptide chains.
65 ter reproductions of the local structures of polypeptide chains.
66 ms the binding interface between interacting polypeptide chains.
67 tively affected the retention of most of the polypeptides chains.
69 mprising 51 residues in two disulfide-linked polypeptide chains, adopts a predominantly alpha-helical
70 re located in different positions within the polypeptide chains, alignment of their structures show t
72 is sp. is heterodimeric, with two homologous polypeptide chains, alpha and beta, derived from a commo
73 Hsp70 that binds ribosome-associated nascent polypeptide chains, also binds to the TPR domain of Sec7
74 els considering the net global charge of the polypeptide chain, although the kinetics of the process
75 f proteins, stabilizing domains, and linking polypeptide chains, although some cases of extracellular
76 known about spontaneous knot formation in a polypeptide chain-an event that can potentially impair i
77 mical protein synthesis to prepare three ShK polypeptide chain analogues, each containing either an a
78 l protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic m
79 acteria and eukaryotes, consists of a single polypeptide chain and contains three major domains: the
80 which either the knot simply slips along the polypeptide chain and falls off the free terminus, or on
81 ification entails partial duplication of the polypeptide chain and mutation of a key catalytic residu
83 0 particle images, shows the trace of the L1 polypeptide chain and reveals how the N- and C-terminal
87 insic dynamic properties of emerging nascent polypeptide chains and guides them toward their biologic
88 Oligomeric interactions between Ca-ATPase polypeptide chains and their modulation by phospholamban
89 ystallography allowing tracing of structural polypeptide chains and visualization of transmembrane pr
90 functional interactions between neighboring polypeptide chains and, in turn, result in increased rat
91 the product of both the overall fold of the polypeptide chain, and, typically, structural motifs mad
92 simulations were started from fully extended polypeptide chains, and no external information was incl
93 ycin is covalently incorporated into nascent polypeptide chains, anti-puromycin immunofluorescence en
96 inct from the fibril lattice even though the polypeptide chains are organized in an immunologically i
98 ngly facilitated incorporation of Ser in the polypeptide chain as compared with selenocysteine at the
99 hat the coarse-graining of the structures of polypeptide chains as self-avoiding tubes can provide an
100 factor (TF) interacts directly with nascent polypeptide chains as they emerge from the ribosome exit
102 ic interactions between various sites in the polypeptide chain, as would occur during the initiation
103 nal Ag-presentation pathways via unprocessed polypeptide chains, as free IGRP206-214 peptide or via p
104 ollagen C-propeptide trimer, where the three polypeptide chains associate together, at the junction w
106 es also revealed a well ordered break in the polypeptide chain at Lys(147), resulting in a large conf
108 genetic modifications are limited to natural polypeptide chains at the Cas9 termini, which excludes a
109 FAD and FMN binding domains within a single polypeptide chain, bacterial NOS is only composed of an
110 signal recognition particle (SRP) recognizes polypeptide chains bearing a signal sequence as they eme
112 mpanied by a fission of the radical-carrying polypeptide chain between the Gly436 and His437 residues
114 ular interactions between the fibril-forming polypeptide chains, but it has so far remained difficult
116 ammals the enzymes are expressed as a single polypeptide chain (CAD) in the order CPS-DHO-ATC and ass
119 hesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that i
120 ich contains a number of routes by which the polypeptide chain can convert its primary sequence into
122 residue hydrophilic, unstructured N-terminal polypeptide chain comprising proline, alanine, and serin
123 at of an overall extended and highly dynamic polypeptide chain comprising three helical segments and
124 as a "cupin" fold, extremely similar both in polypeptide chain conformation and in dimer geometry to
125 well as the effects of the properties of the polypeptide chain connecting the contiguous domains, are
126 irmed that fennel nsLTP1 is a 9433 Da single polypeptide chain consisting of 91 amino acids with eigh
127 -terminal domain and is composed of a single polypeptide chain containing fragment 2 (residues 156-27
129 ind that the topological organization of the polypeptide chain critically determines the folding coop
130 nt change in the mass of any fragment of the polypeptide chain depends uniquely on the rate of exchan
133 and translocates to the periplasm where the polypeptide chain does an about turn in order to enter a
134 -grained, minimalistic representation of the polypeptide chain driven by a structure-based angular po
137 le is known about the progressive folding of polypeptide chains during chain synthesis by the ribosom
138 it the conformational space available to the polypeptide chains during misfolding and fibrillization.
139 including cotranslational folding of nascent polypeptide chains during their synthesis by the ribosom
142 n pausing, roughly at the site where nascent polypeptide chains emerge from the ribosomal exit tunnel
144 the 5-fold axis; residues 81-100 link the 10 polypeptide chains emerging from a 5-fold hub to the N-t
146 hat water can be a good solvent for unfolded polypeptide chains, even those with a hydrophobic and ch
147 hosphorylation of PLB, neighboring Ca-ATPase polypeptide chains exhibit a 4 +/- 2 A decrease in the p
148 ange of experimental techniques suggest that polypeptide chains expand with increasing denaturant con
149 assess the internal scaling behavior of the polypeptide chain, expressed as a mass fractal dimension
151 domain initiates with an extended region of polypeptide chain followed by two turns of an amphipathi
155 We consider the mechanical stretching of a polypeptide chain formed by multiple interacting repeats
156 bacteriophage T4 is synthesized as a single polypeptide chain from a discontinuous reading frame as
157 e novo protein folding by protecting nascent polypeptide chains from misfolding and maintain translat
158 hesizing factories of the cell, polymerizing polypeptide chains from their constituent amino acids.
160 it players can now-starting from an extended polypeptide chain-generate a diversity of protein struct
161 hoice of dye attachment positions within the polypeptide chain has a substantial impact on which unfo
163 ing NMR spectroscopy, we show that the PAGE4 polypeptide chain has local and long-range conformationa
164 plings between amino acids within and across polypeptide chains have allowed for inference of native
165 position, which is expected for an extended polypeptide chain having little or no propensity to form
167 constrains the conformations of the nascent polypeptide chain in a manner not experienced by full-le
168 myloids consist of repetitions of a specific polypeptide chain in a regular cross-beta-sheet conforma
170 onotonic trend between the dimensions of the polypeptide chain in bulk and the degree of compaction:
171 ther, these data suggest that SecA binds the polypeptide chain in its ATP state and releases it in th
173 erage conformational degeneracy of a lattice polypeptide chain in water and quantitatively show that
174 kbone and side chain conformational space of polypeptide chains in a united-residue representation an
179 n permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side
180 odel system for the study of folding of long polypeptide chains, including related phenomena such as
182 se that the two-helix finger of SecA moves a polypeptide chain into the SecY channel with the tyrosin
185 rectly modifying, folding and assembling the polypeptide chains into the native quaternary structure.
186 s simulations revealed that ESI for unfolded polypeptide chains involves protein ejection from nanodr
187 ks via linker sequences into one multivalent polypeptide chain is an elegant alternative to affinity
188 approximately 13 amino acid residues as the polypeptide chain is apparently shortened by approximate
189 uential addition of amino acids to a growing polypeptide chain is carried out by the ribosome in a co
190 donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltrans
191 he compact packing typical of a fully folded polypeptide chain is disrupted and suggest that the incr
192 ect to the distance between hemes, along the polypeptide chain is exactly the same in both redox syst
193 During co-translational folding, the nascent polypeptide chain is extruded sequentially from the ribo
194 ns explored and show that this region of the polypeptide chain is involved in both the nucleation and
195 SecY complex raises the possibility that the polypeptide chain is moved by a two-helix finger domain
197 ore unusually, the N-terminal portion of the polypeptide chain is pinned to the "Kunitz head" by two
198 ng a covalent-loop through which part of the polypeptide chain is threaded (as seen in knotted protei
199 tides are moved by different mechanisms: the polypeptide chain is transferred directly into the chann
200 cid from a non-cognate tRNA into the growing polypeptide chain leads to a general loss of specificity
202 Comparisons are usually performed at the polypeptide chain level, however the functional form of
203 named insulin-like 3 (INSL3) consists of two polypeptide chains linked by two interchain and one intr
204 omplexes between the ligand and the extended polypeptide chain may act as nucleation sites for foldin
205 et been resolved, but the arrangement of the polypeptide chain may have a strong influence on the cap
206 te that tunnel interactions with the nascent polypeptide chain might be relevant for the regulation o
208 m a trefoil knot in the denatured state of a polypeptide chain of 120 residues is 5.8 +/- 1 kcal mol(
209 threonine protein kinase comprising a single polypeptide chain of 4,128 amino acids and belonging to
210 d the potential benefits of reorganizing the polypeptide chain of a protein by circular permutation (
211 e internal redox steps occur within the same polypeptide chain of mammalian QSOX and commence with a
212 ed denatured state we find that knotting the polypeptide chain of MJ0366 increase the folding energy
221 1q is a hexameric molecule assembled from 18 polypeptide chains of three different types encoded by t
223 f multifunctional proteins in which a single polypeptide chain performs multiple biochemical function
224 olvent accessible surface area (SASA) of the polypeptide chain plays a key role in protein folding, c
227 is is the first evidence that folding of the polypeptide chain precedes disulfide formation within a
228 e ring forms a 'gasket-like' seal around the polypeptide chain, preventing the permeation of small mo
229 ge attractions, which can be encoded by both polypeptide chain primary sequence and nucleic acid base
235 specifically an aromatic-rich region of the polypeptide chain (residues 62-70) that has been predict
236 xpression of the corresponding complementary polypeptide chains, retain tetrameric architecture and a
237 er of Escherichia coli SecA interacts with a polypeptide chain right at the entrance into the SecY po
238 e TRAIL protomers were expressed as a single polypeptide chain (scTRAIL), and a novel TRAIL variant,
239 e formation of beta-sheet structures, as the polypeptide chain searches for the native stabilizing cr
240 caffeate acts by disordering precisely those polypeptide chain segments that make up the active site
241 e disulfides spanning a large portion of the polypeptide chain shifts the structure and dynamics of h
243 the plastid envelope and the importing PORA polypeptide chain such that no photoexcitative damage oc
244 re conducted using a single monomer gammaTIM polypeptide chain that folds as a monomer and two gammaT
245 Single-chain FLARE (scFLARE) is a single polypeptide chain that incorporates a transcription fact
247 l slip site generates a force on the nascent polypeptide chain that scales with observed frameshiftin
248 he excluded volume of a local segment of the polypeptide chain that transiently stalls in the nanopor
249 onformationally restricted in regions of the polypeptide chain that ultimately form helices I, II and
250 BoNTs are synthesized as single inactive polypeptide chains that are cleaved by endogenous or exo
251 al machineries for the synthesis of thirteen polypeptide chains that are components of the complexes
252 matic, because immune receptors comprise two polypeptide chains that are encoded by separate mRNAs.
253 but also several further versions of the two polypeptide chains that most likely differ with respect
255 MCM2-7 is a heterocomplex made of different polypeptide chains, the MCM complexes of many Archaea fo
256 n, because sortase A enables the splicing of polypeptide chains, the transpeptidation reaction cataly
257 roEL-GroES sterically confines the unknotted polypeptide chain thereby promoting knotting is unlikely
258 s protein synthesis by accepting the growing polypeptide chain, thereby killing bacterial cells.
259 ding nucleators by preorganizing the pendant polypeptide chains, thereby lowering the activation barr
260 te release and allows passive sliding of the polypeptide chain through the SecA-SecY complex until th
262 suggests a dimeric arrangement of Ca-ATPase polypeptide chains through the proximal association of N
263 lectively oxidizes the N-terminal amine of a polypeptide chain to a ketone or an aldehyde group.
264 te modulates the intrinsic propensity of the polypeptide chain to aggregate and that the algorithm de
266 ifferent icosahedral symmetries, causing the polypeptide chain to exist in seven quasi-equivalent env
267 lix motifs) facilitate bending and allow the polypeptide chain to fold into a hollow circular structu
269 d state presents ample opportunities for the polypeptide chain to transiently sample nonnative struct
270 coarse-grained C(alpha)-side chain model for polypeptide chains to simulate the folding of src SH(3)
271 tudied folding events at the early stages of polypeptide chain translocation into the mammalian ER us
272 alent folding and assembly of macromolecular polypeptide chains, ultimately preventing the formation
273 haracterize the crowding effects on the same polypeptide chain under two drastically distinct folding
276 n a substrate and then translocate along the polypeptide chain, unfolding and degrading protein domai
277 ecause of simplified UNRES representation of polypeptide chains, use of enhanced sampling methods, co
279 The iron hemes of MtrA are bound to its polypeptide chain via proximal (CXXCH) and distal histid
282 and allo-Ile, both l-allo-ShK and d-allo-ShK polypeptide chains were prepared by total chemical synth
283 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
295 n only be measured at high concentrations of polypeptide chains with slow scanning rates, for example
296 le of hindered dihedral rotations within the polypeptide chain, with a proportionality coefficient b
298 gies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromy