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1 voltage-clamp fluorometry with a fluorescent unnatural amino acid.
2 firmed a high translational fidelity for the unnatural amino acid.
3 age C-H oxidation to one containing a linear unnatural amino acid.
4  utilizing protein expressed with an alkynyl unnatural amino acid.
5 or efficiently designing peptides containing unnatural amino acids.
6  post-translational modifications (PTMs) and unnatural amino acids.
7 rature procedures for the syntheses of these unnatural amino acids.
8 ll molecules bearing natural or bioisosteric unnatural amino acids.
9 rocyclic peptides that contain a majority of unnatural amino acids.
10 brary (HyCoSuL), which uses both natural and unnatural amino acids.
11 he engineering of translation to incorporate unnatural amino acids.
12 r facilitate the expression of proteins with unnatural amino acids.
13 which are the most frequently used to encode unnatural amino acids.
14 e beta-barrel as well as the introduction of unnatural amino acids.
15 y in live cells by genetically incorporating unnatural amino acids.
16 the production of mutant proteins containing unnatural amino acids.
17 n through the site-directed incorporation of unnatural amino acids.
18  photostabilizer and biomolecular target via unnatural amino acids.
19 ish eight tripeptides, each having different unnatural amino acids.
20 nalogues in which Phe(13) was substituted by unnatural amino acids.
21 ent structure (7) was replaced by natural or unnatural amino acids.
22                                 Three N-Fmoc unnatural amino acids (1-3) that contain varying linkers
23 es of mutants site-specific labeled with the unnatural amino acid, [(13)C]p-methoxyphenylalanine, in
24 ne WALP24 peptide labeled with the semirigid unnatural amino acid 4-(3,3,5,5-tetra-methyl-2,6-dioxo-4
25     Two stabilized derivatives incorporating unnatural amino acids ((68)Ga-SH01078 and (68)Ga-P03034)
26 ease the utility of protein mutagenesis with unnatural amino acids, a recombinant expression system i
27                            Translations with unnatural amino acids (AAs) are generally inefficient, a
28 noacyl-tRNA synthetase pair specific for the unnatural amino acid added to the media and the protein
29  with the ease of synthesis of the necessary unnatural amino acids allows for facile synthesis of tri
30 er-peptide elements with genetically encoded unnatural amino acids (amino acids that have been artifi
31            The synthesis of a third class of unnatural amino acids, amino tetrazolyl alanines ((ATz)A
32 used biosynthetic methods to incorporate the unnatural amino acid analogue 2-fluorohistidine (2-FHis)
33 ethodology to incorporate a photoactivatable unnatural amino acid and photochemically cleave the back
34 combining mRNA display with incorporation of unnatural amino acids and "click" chemistry.
35 yl-tRNA synthetase-tRNA pairs that recognize unnatural amino acids and decode the new codons.
36 fted toward site-specific modification using unnatural amino acids and engineered site-selective amin
37 n reaction was applied to the preparation of unnatural amino acids and geometrically controlled tri-
38                             Incorporation of unnatural amino acids and peptidomimetic residues into t
39 e optimized this system for use with several unnatural amino acids and provide a demonstration of its
40  parameter and topology files to accommodate unnatural amino acids and the delta amide linkages.
41  on the in vivo incorporation of fluorescent unnatural amino acids and their analysis by steady-state
42           Methods for installing natural and unnatural amino acids and their modifications into prote
43 ing novel self-associating peptides based on unnatural amino acids, and inhibitor peptides of detrime
44 the amino acid sequence, the introduction of unnatural amino acids, and labeling with stable isotopes
45                                          The unnatural amino acid appears to disrupt the interactions
46               Among them, silicon-containing unnatural amino acids are becoming an interesting new cl
47 specifically incorporating multiple distinct unnatural amino acids are hampered by their low efficien
48 bility and unique conformational properties, unnatural amino acids are highly valued by pharmaceutica
49                       In engineered systems, unnatural amino acids are incorporated into proteins to
50 CR1 (1-350) containing Mn(2+) chelated to an unnatural amino acid assists in the characterization of
51 efficiency incorporation of a single type of unnatural amino acid at a time, because every triplet co
52  created a neopeptide via introduction of an unnatural amino acid at the K(12) position, which could
53 eases the yield of protein, incorporating an unnatural amino acid at three sites, from unmeasurably l
54 F1, we increase the yield of protein bearing unnatural amino acids at a single site 17- to 20-fold.
55 ith site-specific incorporation of probes or unnatural amino acids at its N or C termini.
56     A set of variants containing natural and unnatural amino acids at position 15, which were designe
57 ial expression of mutant proteins containing unnatural amino acids at specific sites designated by am
58 l metabolic placement of a uniquely reactive unnatural amino acid, azidohomoalanine (Aha), followed b
59                      We have developed a new unnatural amino acid based on the solvatochromic fluorop
60            The ability to genetically encode unnatural amino acids beyond the common 20 has allowed u
61 ry is applied to the gram-scale syntheses of unnatural amino acids, bioactive molecules, and chiral b
62 roperties allow them to incorporate multiple unnatural amino acids (but not natural amino acids), wou
63 late an amber suppressor tRNA with a desired unnatural amino acid, but no natural amino acids, in euk
64 ns that are involved in the synthesis of the unnatural amino acid by genetic analysis.
65                     In vivo incorporation of unnatural amino acids by amber codon suppression is limi
66 r demonstrate that IQF substrates containing unnatural amino acids can be used to investigate proteas
67 his study demonstrates that incorporation of unnatural amino acids can provide a flexible, straightfo
68 128, with a range of alternative natural and unnatural amino acids, changed the EC50 (from approximat
69  it will be possible to encode more than 200 unnatural amino acid combinations using this approach.
70  improved second-generation synthesis of the unnatural amino acid components of the anticancer peptai
71 s enabled a significant increase in yield of unnatural amino acid containing proteins from tens of mi
72 i-Miyaura coupling of genetically positioned unnatural amino acids containing aryl halide side chains
73                          Genetically encoded unnatural amino acids could facilitate the design of pro
74 -linking coupled with mass spectrometry, and unnatural amino acid cross-linking.
75 2 substrate library, which also included the unnatural amino acid cyclohexylalanine (Cha) derivative
76 d glycine in the selectivity filter with the unnatural amino acid d-Alanine.
77  metathesis as key steps to assemble various unnatural amino acid derivatives and peptides.
78 sters, which may be regarded as novel hybrid unnatural amino acids, during the peptide synthesis itse
79 g selective modification of both natural and unnatural amino acids--each with merits and limitations-
80           We used mutations with natural and unnatural amino acids, electrophysiological recordings,
81 estrict the incorporation of the fluorescent unnatural amino acid epsilonNH2-Bodipy576/589-lysine (BO
82  apoA-I specifically designed to include the unnatural amino acid exclusively at position 166.
83                                    Moreover, unnatural amino acid expression in the methylotrophic ho
84 h residues were substituted with natural and unnatural amino acids, focusing on the role of aromatici
85 ilitate new molecular studies using tailored unnatural amino acids for cell biology and neurobiology.
86 sical properties of three of the fluorescent unnatural amino acids from two classes were also studied
87 ledge, successful detection of a fluorescent unnatural amino acid (fUAA), Lys(BODIPYFL), incorporated
88 te-specifically incorporate a diverse set of unnatural amino acids (>30) into proteins and quickly ad
89 elanogaster) and the incorporation of useful unnatural amino acids has been aided by the development
90          Using this system multiple distinct unnatural amino acids have been incorporated and used to
91 ty filter region of the NaK channel with the unnatural amino acids homoserine and cysteine sulfonic a
92             As well, using a UV-crosslinking unnatural amino acid in KCNE1, we found EQQQQ and EQQ cr
93 ssible to genetically encode a wide array of unnatural amino acids in both prokaryotic and eukaryotic
94 w one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic
95 ade possible the genetic encoding of diverse unnatural amino acids in different mammalian cells and p
96 highlight the utility of genetically encoded unnatural amino acids in exploring the effects of posttr
97 ursors at 254 nm gave access to the required unnatural amino acids in good yields.
98 synthesis of therapeutic proteins containing unnatural amino acids in mammalian cells.
99                    The incorporation of both unnatural amino acids in place of a phenylalanine in the
100 ally-encoded, site-specific incorporation of unnatural amino acids in regions essential for activatio
101 in P. pastoris and used to incorporate eight unnatural amino acids in response to an amber codon with
102 e to efficiently direct the incorporation of unnatural amino acids in response to quadruplet codons.
103  have been evolved to incorporate a range of unnatural amino acids in response to the amber codon in
104 o pEVOL and compared their ability to insert unnatural amino acids in response to three independent a
105 o-Q1 we direct the incorporation of distinct unnatural amino acids in response to two of the new blan
106 rrounding residues but have not incorporated unnatural amino acids in this process.
107 nd enables the preparation of Fmoc-protected unnatural amino acids in three steps.
108 including the site-specific incorporation of unnatural amino acids in vivo and the directed evolution
109        Receptors rescued by incorporation of unnatural amino acids, including p-benzoyl-l-phenylalani
110            With this new system, a number of unnatural amino acids, including the photocrosslinkers p
111 arnessing proximity-enabled reactivity of an unnatural amino acid incorporated in the bait toward a t
112                                  Here, using unnatural amino acid incorporation and fluorine-19 nucle
113 ent advances are enhancing the efficiency of unnatural amino acid incorporation by creating and evolv
114 nstrate that tRNA levels can be limiting for unnatural amino acid incorporation efficiency, and we de
115 ns and highlight the exceptional capacity of unnatural amino acid incorporation for increasing our un
116  we increase the efficiency of site-specific unnatural amino acid incorporation from approximately 20
117 don suppression and related technologies for unnatural amino acid incorporation has greatly expanded
118 n O-ribosome previously evolved for enhanced unnatural amino acid incorporation in response to amber
119                            The efficiency of unnatural amino acid incorporation in response to the am
120 codons, to provide a substantial increase in unnatural amino acid incorporation in response to the UA
121                                              Unnatural amino acid incorporation into ion channels has
122                       Improving the yield of unnatural amino acid incorporation is an important chall
123 ress in this area: (i) the low efficiency of unnatural amino acid incorporation that limits labeling
124  of the nonsense suppression methodology for unnatural amino acid incorporation to probe drug-recepto
125 f truncated proteins in experiments that use unnatural amino acid incorporation to probe protein func
126 enesis and the high precision methodology of unnatural amino acid incorporation to study the gating i
127 nstituted in vitro translation, quantitative unnatural amino acid incorporation via AUG codon reassig
128                                        Using unnatural amino acid incorporation, we demonstrate the r
129 m Methanococcus janaschii Tyr synthetase for unnatural amino acid incorporation.
130 nto the factors that control the fidelity of unnatural amino acid incorporation.
131 transfer RNA (tRNA) synthetase/tRNA pair for unnatural amino acid incorporation.
132 en used to site-specifically incorporate the unnatural amino acid into a protein in mammalian cells i
133 ite-specific incorporation of an immunogenic unnatural amino acid into a protein of interest produces
134 ite-specific incorporation of an immunogenic unnatural amino acid into an autologous protein offers a
135 pair enabling site-specific insertion of the unnatural amino acid into apoA-I.
136 ciently and site-specifically incorporate an unnatural amino acid into proteins.
137      In the present work, we incorporated an unnatural amino acid into the alpha-hemolysin (alphaHL)
138 d by the introduction of an azide-containing unnatural amino acid into the coat protein for the first
139 er RNAs to encode numerous pairs of distinct unnatural amino acids into a single protein expressed in
140 t of their kind to show the incorporation of unnatural amino acids into a voltage-gated sodium channe
141            We independently incorporated six unnatural amino acids into GFP expressed in CHO cells wi
142 n vivo incorporation of isotopically labeled unnatural amino acids into large proteins drastically re
143      However, the efficient incorporation of unnatural amino acids into proteins and the specific, fl
144 h mutually orthogonal methods of introducing unnatural amino acids into proteins as well as with chem
145  new vector, pEVOL, for the incorporation of unnatural amino acids into proteins in Escherichia coli
146 nse, rare, or 4-bp codons to incorporate >50 unnatural amino acids into proteins in Escherichia coli,
147 The efficient, site-specific introduction of unnatural amino acids into proteins in mammalian cells i
148  that enables the efficient incorporation of unnatural amino acids into proteins in mammalian cells.
149 erein we review work on the incorporation of unnatural amino acids into proteins in response to quadr
150  to allow the site-specific incorporation of unnatural amino acids into proteins in response to the a
151  that specifically prevents incorporation of unnatural amino acids into proteins may provide a new st
152 n for the incorporation of multiple distinct unnatural amino acids into proteins or the synthesis and
153               Site-specific incorporation of unnatural amino acids into proteins provides a powerful
154          To encode efficiently many distinct unnatural amino acids into proteins we require blank cod
155 sion, for the site-specific incorporation of unnatural amino acids into proteins, is currently limite
156  principles and methods for incorporation of unnatural amino acids into proteins.
157 een used to enable the incorporation of many unnatural amino acids into recombinant proteins in vivo.
158 bles efficient, homogeneous incorporation of unnatural amino acids into target proteins in diverse ma
159 e basis for ion selectivity by incorporating unnatural amino acids into the channel, engineering chan
160 prove useful for the incorporation of bulky, unnatural amino acids into the genetic code.
161 ction may provide a way for incorporation of unnatural amino acids into tRNA, and consequently into p
162 e ethynyl group of pENPhe suggests that this unnatural amino acid is a more conservative substitution
163 nt synthesis of products containing multiple unnatural amino acids is challenging.
164 urements, because efficient incorporation of unnatural amino acids is limited to transient expression
165 ural changes, since the incorporation of the unnatural amino acids is not inherently limited by the s
166 anted to report the utility of an unexplored unnatural amino acid, isothiocyanyl alanine ((NCS)Ala =
167 ed have been evolved to incorporate numerous unnatural amino acids, it will be possible to encode mor
168 or labeling through genetic incorporation of unnatural amino acids, lanthanide resonance energy trans
169                    This paper introduces the unnatural amino acids m-Abc(2K) and o-Abc(2K) as nanomet
170  been made to peptides, including the use of unnatural amino acids, mainchain modifications and other
171 ension of approaches to incorporate multiple unnatural amino acids may allow the combinatorial biosyn
172         Using next-generation sequencing and unnatural amino acid-mediated protein-DNA cross-linking,
173                          This method uses an unnatural amino acid-modified Src homology 2 (SH2) domai
174                          We report a general unnatural amino acid mutagenesis approach to quantify th
175 ge-gated ion channels that have emerged from unnatural amino acid mutagenesis approaches.
176       Previous studies have established that unnatural amino acid mutagenesis can probe three key bin
177                                  Here we use unnatural amino acid mutagenesis coupled with agonist an
178          Here we probe the role of D89 using unnatural amino acid mutagenesis coupled with electrophy
179 nto AMPA receptors using genetically encoded unnatural amino acid mutagenesis in a mammalian cell lin
180 hotocaging of a synthetic gene network using unnatural amino acid mutagenesis in mammalian cells was
181                                     Further, unnatural amino acid mutagenesis is used to replace the
182 recision structural modifications enabled by unnatural amino acid mutagenesis on mammalian receptors
183                                              Unnatural amino acid mutagenesis provides the wherewitha
184                                  Here we use unnatural amino acid mutagenesis to characterize binding
185                                  Here we use unnatural amino acid mutagenesis to examine the ligand b
186 here we use double mutant cycle analysis and unnatural amino acid mutagenesis to probe the functional
187    The work described here on application of unnatural amino acid mutagenesis to two GPCRs, the chemo
188 oteins expressed in Escherichia coli through unnatural amino acid mutagenesis using a Cnf-specific tR
189 tives into the receptor binding pocket using unnatural amino acid mutagenesis, and evaluating the res
190 ompared with previously reported vectors for unnatural amino acid mutagenesis.
191                                        Using unnatural amino-acid mutagenesis, we subtly altered the
192 ereoselective route to a masked form of this unnatural amino acid now enabled the synthesis of two of
193  to this problem, we genetically encoded the unnatural amino acids o-nitrobenzyl-2-fluorotyrosine, -3
194 o selectively aminoacylate its tRNA with the unnatural amino acid of interest.
195 cids, the necessity for the incorporation of unnatural amino acids or chemical modification of the pr
196      In this method, the genetically encoded unnatural amino acid p-acetyl-L-phenylalanine (p-AcPhe)
197  For these studies, we have incorporated the unnatural amino acid p-acetyl-L-phenylalanine for specif
198                                          The unnatural amino acid p-acetylphenylalanine (pAcF) was si
199            First, we genetically encoded the unnatural amino acid p-azido-L-phenylalanine (azF) at va
200           By replacing LptD residues with an unnatural amino acid p-benzoyl-L-phenyalanine (pBPA) and
201 n suppression to introduce the photoreactive unnatural amino acid p-benzoyl-l-phenylalanine (BzF) at
202        By site-specific incorporation of the unnatural amino acid p-benzoyl-L-phenylalanine, a photor
203 incorporation of the UV photo-cross-linkable unnatural amino acid p-benzoyl-L-phenylalanine.
204                                          The unnatural amino acid p-Benzoylphenylalanine was successf
205                 Here we demonstrate that the unnatural amino acid p-boronophenylalanine (BF) confers
206       The site-specific incorporation of the unnatural amino acid p-nitrophenylalanine (pNO(2)Phe) in
207                          We incorporated the unnatural amino acids p-acetyl-L-phenylalanine (Acp) and
208 We have developed a method to incorporate an unnatural amino acid, p-acetylphenylalanine (pAcPhe) int
209 ated to a mutant alphaCD3 Fab containing the unnatural amino acid, p-acetylphenylalanine, at a define
210 CLL1-alphaCD3, using the genetically encoded unnatural amino acid, p-acetylphenylalanine.
211 C identical withN stretching vibration of an unnatural amino acid, p-cyano-phenylalanine, to directly
212                                          The unnatural amino acid para-azido-L-phenylalanine was inco
213                           Here, we have used unnatural amino acid photo-cross-linking to investigate
214                             By incorporating unnatural amino acid photochemical and new click-chemica
215 h nanomaterials by targeted incorporation of unnatural amino acids possessing dual affinity to differ
216 es rely mainly on traditional coupling using unnatural amino acids, postsynthetic modification of pep
217                             Thus, an encoded unnatural amino acid produces a chemical "handle" by whi
218  The methodology establishes novel routes to unnatural amino acids, proline homologues, and cyclic vi
219  not be feasible to separate the full-length unnatural amino acid protein from the truncated form.
220                          Genetically encoded unnatural amino acids provide powerful strategies for mo
221 mination of a chiral center derived from the unnatural amino acid R-alpha-methylcysteine makes the mo
222 gth overlap and highly selective natural and unnatural amino acid recognition sequences.
223 e first experimental evidence documenting an unnatural amino acid replacement in a GPCR expressed in
224 tural amino acids will extend the use of the unnatural amino acid replacement methodology to amino ac
225 o acids are transformed to twenty-one chiral unnatural amino acids representing seven distinct functi
226 e site specifically inserted a (13)C-labeled unnatural amino acid residue, (13)C-p-methoxyphenylalani
227        Many important and useful natural and unnatural amino acid salts can be produced in excellent
228    This approach provides hybrid natural and unnatural amino acid sequences, and thus we termed it th
229 llows selection to yield proteins containing unnatural amino acids should such sequences functionally
230 This Perspective highlights the diversity of unnatural amino acid structures found in hit-to-lead and
231                                        Using unnatural amino acid substitution and a standard linkage
232 sized a library of 61 individual natural and unnatural amino acids substrates, chosen to cover a broa
233  achieved using peptide libraries containing unnatural amino acids such as the hybrid combinatorial s
234 ombination of self-labeling protein tags and unnatural amino acid technology permits the semisynthesi
235                                              Unnatural amino acid technology provides a degree of bio
236 he binding site of the binding protein using unnatural amino acid technology.
237                                           An unnatural amino acid termed a proline-templated glutamic
238             O-tert-Butyltyrosine (Tby) is an unnatural amino acid that can be site-specifically incor
239                 Bpa is a photoaffinity label unnatural amino acid that can form covalent bonds with a
240                   Specifically, we report an unnatural amino acid that preferentially labels amine-pr
241 otein an appropriately "tuned" electrophilic unnatural amino acid that reacts with a native nucleophi
242 eted cellular proteins with versions bearing unnatural amino acids that allow imaging or synthetic re
243  bacteria, limiting the types and numbers of unnatural amino acids that can be utilized at any one ti
244 lational, site-specific incorporation of two unnatural amino acids that can function as fluorescence
245              We show, using a photoreactive, unnatural amino acid, that Asf1 tail residue 210 cross-l
246                      Here, we incorporate an unnatural amino acid, thia-methylimidazole, at this site
247  Ita), for the synthesis of another class of unnatural amino acids, thioureayl alanines ((TU)Ala = Tu
248        The expression of proteins containing unnatural amino acids through suppression of a stop codo
249 addition, SIDEpro can accommodate any PTM or unnatural amino acid, thus providing a flexible predicti
250  that binds to the hot spot, and selected an unnatural amino acid to incorporate, based on the struct
251 f covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine.
252 redoxins, and demonstrate the power of using unnatural amino acids to address critical chemical biolo
253 of His-66 may improve the ability of certain unnatural amino acids to be incorporated by the ribosome
254 tantially enhanced this by incorporating 102 unnatural amino acids to explore the S1-S4 pockets of hu
255     This method entails the incorporation of unnatural amino acids to site-specifically label protein
256 ta suggest not only robust methods for using unnatural amino acids to study large proteins by NMR but
257         The stereoselective synthesis of the unnatural amino acid tubuvaline is accomplished using te
258            Using only between 8 and 25 mg of unnatural amino acid, typically 2 mg of FAS-TE, sufficie
259       In our system, any genetically encoded unnatural amino acid (UAA) can be used as a small-molecu
260 aviolet irradiation of a photo-crosslinkable unnatural amino acid (UAA) cotranslationally incorporate
261                     Genetically incorporated unnatural amino acid (UAA) technologies are powerful too
262 ally introduced into proteins by enabling an unnatural amino acid (Uaa) to selectively react with a p
263 ptor by genetically encoding a photoreactive unnatural amino acid (UAA).
264 essential HIV-1 protein biosynthesis through unnatural amino acid (UAA*)-mediated suppression of geno
265 r optical control of neuronal proteins using unnatural amino acids (Uaa) in vivo is lacking.
266                   The ability to incorporate unnatural amino acids (UAA) into proteins in a site spec
267 nsporter protein to encode photocrosslinking unnatural amino acids (UAAs) into 75 different positions
268           The site-specific incorporation of unnatural amino acids (UAAs) into proteins in living cel
269 The ability to site-specifically incorporate unnatural amino acids (UAAs) into proteins is a powerful
270               Site-specific incorporation of unnatural amino acids (UAAs) into proteins is a valuable
271 rm is reported that enables incorporation of unnatural amino acids (UAAs) into specific sites on the
272  click chemistry and the genetic encoding of unnatural amino acids (UAAs) to overcome this limitation
273  has led to the addition of approximately 70 unnatural amino acids (UAAs) to the genetic codes of Esc
274                           Here, we show that unnatural amino acids (UAAs) with orthogonal chemical re
275                                  Fluorescent unnatural amino acids (UAAs), when genetically incorpora
276 onal aaRS to distinguish between a favorable unnatural amino acid (unAA) substrate from unfavorable n
277 hydrate-binding proteins that use a reactive unnatural amino acid "warhead" and demonstrates that a "
278 ogonal tRNA-synthetase pair, the fluorescent unnatural amino acid was incorporated in the Shaker volt
279 s for genetically directing incorporation of unnatural amino acids, we have inserted trifluoromethyl-
280 s-linking experiments with photo-activatable unnatural amino acids, we show that full-length BACE1, i
281  Saccharomyces cerevisiae to be specific for unnatural amino acids were inserted between eukaryotic t
282                                              Unnatural amino acids were introduced by chemical synthe
283  the catalytic cycle can be maintained using unnatural amino acids, which may prove useful in enzyme
284 f high yields of complex proteins containing unnatural amino acids whose expression is not practical
285 application of a peptide delivery system for unnatural amino acids will extend the use of the unnatur
286                      The genetic encoding of unnatural amino acids will remove this restriction and e
287 arget protein contains a genetically encoded unnatural amino acid with bioorthogonal reactivity and t
288  antibodies containing a genetically encoded unnatural amino acid with orthogonal chemical reactivity
289                  We genetically encoded four unnatural amino acids with a diverse set of functional g
290 mized system, we produce proteins containing unnatural amino acids with comparable yields to a protei
291 e access to two conformationally constrained unnatural amino acids with different dispositions of the
292 eral strategy for labelling pairs of encoded unnatural amino acids with different probes via rapid an
293  labeling of proteins at genetically encoded unnatural amino acids with distinct small molecules at p
294  We developed a general approach that allows unnatural amino acids with diverse physicochemical and b
295  Using this new methodology, we incorporated unnatural amino acids with extended side chains into the
296  site-specific incorporation of a variety of unnatural amino acids with novel chemical and biological
297 e demonstrate the use of genetically encoded unnatural amino acids with orthogonal chemical reactivit
298 s were constructed using genetically encoded unnatural amino acids with orthogonal chemical reactivit
299                             The synthesis of unnatural amino acids with small side-chain functionalit
300                             Incorporation of unnatural amino acids with unique chemical functionaliti

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