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1 TFE also decreased the level of solubility of the peptid
2 TFE and ammonium perfluoro-octanoate exposures were high
3 TFE appears to induce the fibrils by stabilizing a beta-
4 TFE concentrations matching an alpha-helical content of
5 TFE increased the alpha-helical contribution of wild-typ
6 TFE operates via allosteric and direct mechanisms.
7 TFE unfolds VlsE at low percentages but promotes the for
8 TFE-fusion renal cell carcinomas (TFE-fusion RCCs) are c
9 TFE-induced conformational changes in the monomer protei
11 Negative ion mode spray stability with 0.2% TFE is approximately 6x higher than for strictly aqueous
15 vation kinetics were conducted by reacting 2(TFE)-(13)C with 300-1000 psi of methane in single-crysta
16 n methanol (2(MeOD)) and trifluoroethanol (2(TFE)) adducts, with methanol binding preferentially (K(e
20 role in the mechanism of aggregation in 25% TFE, but also from mutations located in other regions.
21 propensity increases regularly from 0 to 25% TFE but levels off at higher TFE concentrations, which e
25 studies of both peptides in saturating (43%) TFE reveal stable alpha-helices from Gly500 to Lys522, b
27 the sample to give a solution containing 5% TFE, the fraction of partially unfolded monomeric protei
28 rate of disaggregation of protofibrils in 5% TFE result not only from mutations situated in the regio
29 gh-resolution structures obtained with 50:50 TFE/water revealed that all three analogs display two he
30 +) in the presence of the CTAB than in a 50% TFE solution (K(d) = 3.1 x 10(-4) M in CTAB and 2.3 x 10
35 t thermal denaturation of the peptide in 50% TFE containing 1 mM Zn(2+) was associated with both enth
38 of hydrogen exchange for the peptide in 50% TFE-d, are consistent with such a model, the maximum pro
47 ween spin labels located at i and i + 4 in a TFE/H(2)O mixture or a POPC bilayer is indicative of an
48 B(1)(T377-E416) peptide reconstituted into a TFE/H(2)O mixture or a POPC or DMPC bilayer were estimat
50 ghest helix propensity at 0 degrees C in all TFE concentrations, it is lower than Leu, Ile, and Val a
55 nt (kH) were measured on going from MeOH and TFE to isooctane (kH(isooctane)/kH(MeOH) = 5-12; kH(isoo
56 rillization kinetics depended on peptide and TFE concentrations, and had a nucleation step followed b
58 he higher reaction rates observed in TFA and TFE compared with CH2Cl2 arise from stabilization of the
62 entification of the beta-subunit of archaeal TFE enabled us to reconstruct the evolutionary history o
66 we introduce (19)F, in this case from bound TFE, as a new probe for the binding of small molecules t
67 The (19)F and (2)H ENDOR spectra of bound TFE together with (1,2)H ENDOR spectra of bound ethanol
72 so give curves of helix formation induced by TFE at constant temperature, and the properties of these
73 e slow structural change of Con A induced by TFE provides a useful model system for study of protein
74 ic disorder that is substantially reduced by TFE, but a significant gradient in dynamics is observed,
76 cular hydrogen bonds are not strengthened by TFE and that amide hydrogen bonds in the transition stat
78 of thermal unfolding curves in concentrated TFE solutions results from the decrease of the enthalpy
80 f a transcription activator, here designated TFE, that may be universally present in the Archaea.
83 tion factor B (TFB), transcription factor E (TFE) and the 12-subunit RNA polymerase (RNAP) from Metha
85 anisms of the basal transcription factors E (TFE) and Spt4/5 through conformational constraints has r
86 ts the results for the four peptides at each TFE concentration; only two of the basic helix-coil para
87 lculations indicate that the solvent, either TFE or HFIP, can stabilize the transition state through
88 ive to backbone fluctuations and that either TFE or calcium binding stabilizes the secondary structur
89 ) working electrodes: a thin-film electrode (TFE), a screen-printed electrode (SPE), and a microarray
92 nd also subunit E and a transcription factor TFE that co-purifies with RNAP from wild-type cells, but
93 ctions with the general transcription factor TFE, as well as with the transcriptional activator Ptr2.
94 nated alcohol varied from 53:47 to 87:13 for TFE, 60:40 to 92:8 for HFP, and 52:48 to 73:27 for PFTB.
95 emained unchanged ( approximately 40:60) for TFE and for PFTB over the range of 25-250 molar equiv.
96 xposure matrix (1950-2002) was developed for TFE and ammonium perfluoro-octanoate, a chemical used in
97 such a term greatly improves the fitting for TFE, MeCN/H(2)O 2:1, and MeOH but at the expense of that
98 rmylphenylalanine trifluoroethyl ester (fPhe-TFE) represents an improvement over earlier model reacti
99 ncatalyzed reaction of glycinamide with fPhe-TFE proceeds with a second-order rate constant of 3 x 10
100 he helix-forming properties of peptides from TFE/H2O mixtures (TFE = 2,2, 2-trifluoroethanol) back to
104 y from 0 to 25% TFE but levels off at higher TFE concentrations, which explains why the extent of hel
110 MR studies performed on elbow and elbow-A in TFE indicate that the helical structure is confined to t
112 clude that initiation of EGFP aggregation in TFE likely involves overcoming of multiple protective fa
114 water, but Ser2 affects the conformation in TFE-rich solution in much the same way as Ser5-->Ala sub
116 reover, the increase in the rate constant in TFE is consistent with the observed decrease in donor-ac
117 lical structures in the peptide fragments in TFE was correlated with the observation of turn and/or h
118 gment with the highest degree of helicity in TFE corresponded with the single (alpha-helix in native
121 mpound, salicylic acid, has been measured in TFE/H2O mixtures from the pKa difference between salicyl
127 e peptides show an increase in beta-sheet in TFE, a known inducer of alpha-helices, relative to that
128 asing entropic costs of protein solvation in TFE-water mixtures may both cause the population of the
131 of hydrogen bond strength versus increasing TFE concentration matches both in shape and magnitude th
133 m with the natively disordered state at low [TFE] and with a highly alpha-helical conformation at hig
134 e microphthalmia/transcription factor E (MiT/TFE) family, are similarly regulated during mitophagy.
137 global metabolite profiling reveals that MiT/TFE-dependent autophagy-lysosome activation is specifica
141 results illuminate a pathway leading to MiT/TFE transcription factor activation, distinct from starv
143 1 required for a direct interaction of MITF-TFE factors and E-box 2 for binding of the as yet uniden
145 e suggest that VMD2 is regulated by the MITF-TFE family through two E-boxes, with E-box 1 required fo
147 roperties of peptides from TFE/H2O mixtures (TFE = 2,2, 2-trifluoroethanol) back to water, the therma
150 ter-directed transcription in the absence of TFE, which alleviates this effect by displacing Spt4/5 f
154 brium CD results show that, upon addition of TFE, low-concentration Con A transforms to a highly alph
161 In the presence of low concentrations of TFE, fibril formation is observed in Abeta samples at na
163 mine whether the helix-stabilizing effect of TFE arises from strengthening the hydrogen bonds in the
167 o the DEs (1 or 2) in over 25 molar equiv of TFE occurred highly stereoselectively to afford only cis
168 r, we report the IR spectra as a function of TFE concentration for an alanine-rich peptide based on t
169 s to reconstruct the evolutionary history of TFE/TFIIE-like factors, which is characterised by winged
170 ysical studies have revealed the position of TFE/TFIIE within the pre-initiation complex (PIC) and il
171 ion of 2D NMR experiments in the presence of TFE or DPC micelles, complete 1H NMR assignments of the
174 D) to analyze the CD data in the presence of TFE, by fully assigning the unbound IA(3) protein by NMR
175 (3) become more dispersed in the presence of TFE, indicating that the protein undergoes an unstructur
180 a linear dependence of ln <w> and DeltaH on TFE molarity can be used to extrapolate the results from
183 ere measured between 0 and 50 volume percent TFE and were fitted to the modified Lifson-Roig theory.
184 arrows the range of uncertainty on potential TFE carcinogenicity but cannot conclusively confirm or r
186 , methanol, and dimethyl ether by [(N-N)PtMe(TFE-d(3))](+) ((N-N) = ArN=C(Me)-C(Me)=NAr; Ar = 3,5-di-
193 uoroethylene (CTFE) and tetrafluoroethylene (TFE) were determined in the temperature range 240-340 de
196 s, is important in promoter opening and that TFE can compensate for defects in the N terminus through
199 uncation mutant alphaS1-102, indicating that TFE-induced structural transitions involve the N terminu
201 Several recent papers have proposed that TFE acts by selectively desolvating the peptide backbone
204 g site with few intermolecular contacts, the TFE-inducible alphaB motif is deeply engaged in a hydrop
206 ensive secondary structure is present in the TFE-denatured state but not in the protein denatured in
207 f dark respiration (Rd ) was elevated in the TFE-treated forest trees relative to the control by 28.2
210 ) to elucidate both the main features of the TFE-driven transition and the residue-level deviations f
211 ly helical intermediate is on-pathway to the TFE-induced formation of both the highly helical monomer
212 TFE fibrils is strongly correlated with the TFE-induced formation of a monomeric, partly helical int
213 tates upon association with membranes, these TFE-induced conformations imply relevant pathways for me
214 We find that efficient production of these TFE fibrils is strongly correlated with the TFE-induced
222 nding of ethanol and 1,1,1-trifluoroethanol (TFE) to both the H(mv) and H(ox) forms of soluble methan
223 egation in 25% (v/v) 2,2,2 trifluoroethanol (TFE) are different from those that promote disaggregatio
226 ow concentrations of 2,2,2-trifluoroethanol (TFE) convert predominately unstructured Abeta monomers i
227 formed in 60% (v/v) 2,2,2-trifluoroethanol (TFE) has been studied using hydrogen exchange pulse labe
228 solutions containing 2,2,2-trifluoroethanol (TFE) have shown that the formation of structural interme
233 in water and in 23% 2,2,2-trifluoroethanol (TFE) shows that the individual residue cross peaks of IA
235 n in the presence of 2,2,2-trifluoroethanol (TFE), a solvent known to stabilize hydrogen bonds within
236 osolvents, including 2,2,2-trifluoroethanol (TFE), on the thermodynamics and kinetics of folding of t
240 solvent system (40% 2,2,2-Trifluoroethanol (TFE)/water), which gave the largest structural differenc
241 In the presence of 25% trifluoroethanol (TFE), the helicity of the peptide is 80% and the kobs in
242 pha-helical content in 30% trifluoroethanol (TFE) or in dodecylphosphocholine (DPC) micelles, which m
244 ndary structure, while 40% trifluoroethanol (TFE) induces >90% helicity and is unperturbed by the spi
246 duced by dissolving in 50% trifluoroethanol (TFE) were monitored at neutral and low pH by far- and ne
249 n the fluorinated alcohols trifluoroethanol (TFE), hexafluoropropan-2-ol (HFP), and perfluoro-tert-bu
251 uoroisopropanol (HFIP) and trifluoroethanol (TFE), to activate the electron-deficient heterocyclic az
255 lar dichroism (CD) in H2O, trifluoroethanol (TFE), and SDS micelles confirmed the importance of the a
259 as well as the ability of trifluoroethanol (TFE) and detergent systems to induce secondary structure
262 d in vitro, by addition of trifluoroethanol (TFE), into amyloid fibrils of the type observed in a ran
263 moderate concentrations of trifluoroethanol (TFE), or because of the appearance of a highly alpha-hel
269 the presence of 25% (v/v) trifluoroethanol (TFE) AcP undergoes partial unfolding and globular aggreg
271 acid chlorides in 97% w/w trifluoroethanol (TFE)-water spanning over 10 (9) in rate constant at 25 d
276 OH) and fluorinated (i.e., trifluoroethanol, TFE) alcohols on the secondary structure and thermodynam
278 shed new light on the mechanisms underlying TFE-fusion RCCs and suggest a possible therapeutic strat
279 aximum of approximately 55% helix at 50% v/v TFE, corresponding to approximately 100% helix in the D-
280 n kinetic behavior upon addition of 5% (v/v) TFE indicates that it stabilizes the transition state to
281 ta (1-42), we started our studies in various TFE-water mixtures and found striking differences betwee
282 ns where the peptides are most folded (water/TFE, 5 degrees C), tau(ex) values for all residues in ea
283 oism and by 2D-NMR in the presence of water; TFE/water; SDS micelles; and in the presence of both neu
285 circular dichroism data to a model in which TFE-water mixtures are assumed to be ideal solutions, we
287 is latter intermediate at -78 degrees C with TFE occurs selectively at the vinyl CH(2) closer to the
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