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1 sence of protein denaturants (4.0 M urea and guanidinium chloride).
2 unfolding intermediate at approximately 1 M guanidinium chloride.
3 rescence at relatively low concentrations of guanidinium chloride.
4 unfolding of the protein in the presence of guanidinium chloride.
5 ns are featureless, statistical coils in 6 M guanidinium chloride.
6 toward thermal denaturation and unfolding by guanidinium chloride.
7 dary and tertiary structure by the chaotrope guanidinium chloride.
8 po alpha-lactalbumin following dilution from guanidinium chloride.
9 e examined for resistance to denaturation by guanidinium chloride.
10 tide were reconstituted by renaturation from guanidinium chloride.
11 guanidinium sulfate has a similar effect to guanidinium chloride.
12 rates of native RNase A in the range 0-0.7 M guanidinium chloride.
13 ns, as indicated by equilibrium unfolding in guanidinium chloride.
14 pe myoglobin were unfolded by titration with guanidinium chloride.
15 crose, 1.0 M glycine, 0.5 M, 1.0 M, or 2.0 M guanidinium chloride, 10% glycerol, or 0.5 M NaCl over a
16 f gyration, 34-35 A, is unchanged from 0-6 M guanidinium chloride and from 20-90 degrees C at pH 2.5,
17 ybrids by denaturing pairs of enzymes in 1 M guanidinium chloride and renaturing them by removing the
18 nsition proceeded at lower concentrations of guanidinium chloride and the second transition proceeded
19 he mechanism by which the aqueous cosolvents guanidinium chloride and urea denature proteins is a mat
20 een hydrophobic and ionic species in aqueous guanidinium chloride and urea solutions using molecular
21 Under strong denaturing conditions (e.g. 6 m guanidinium chloride) and in the presence of a thiol ini
22 Here, we use effects of denaturants (urea, guanidinium chloride) and temperature on folding and unf
23 e spectra, stability towards denaturation by guanidinium chloride, and stability of phosphorylated en
24 turant concentrations varying from 1.5-6.0 M guanidinium chloride are in excellent agreement, with an
25 .4 nm in diameter), and a high concentration guanidinium chloride buffer enables unidirectional, sing
26 s monitored as a function of temperature and guanidinium chloride concentration, and the resulting fr
29 s identical for the two unfolded proteins at guanidinium chloride concentrations >3 M, and the FRET-d
32 the actual decrease is approximately 3 A on guanidinium chloride denaturant dilution from 7.5 to 1 M
34 by CD, the enzyme is less stable to heat and guanidinium chloride denaturation than the wild-type.
37 ears to be a stronger denaturant than GdmCl (guanidinium chloride), even though GdmCl is typically tw
47 well established that low concentrations of guanidinium chloride (GdmCl) inhibit the ATPase activity
48 ons of chemical denaturants such as urea and guanidinium chloride (GdmCl) proteins expand to populate
49 r basis for protein denaturation by urea and guanidinium chloride (GdmCl) should accommodate the obse
51 kinetic thiol-labeling experiments, that the guanidinium chloride (GdmCl)-induced unfolding of RNase
58 the unfolding of cytochrome c and azurin by guanidinium chloride (GuHCl) are used to construct free-
59 mine unfolding intermediates associated with guanidinium chloride (GuHCl)-induced protein denaturatio
60 The known folding rate of 20 s-1 at 1.5 M guanidinium chloride in 400 microM Zn2+ provides an uppe
61 are linearly dependent on concentrations of guanidinium chloride in the measurable range from 1.7 to
62 reases linearly as [C] (the concentration of guanidinium chloride) increases with the slope, m, that
63 rant are four times larger than those in 6 M guanidinium chloride, indicating a decrease in the avera
64 the toxoid underwent thermal-, low-pH-, and guanidinium chloride-induced conformational changes only
65 o be very unstable on the basis of urea- and guanidinium chloride-induced denaturation studies monito
69 d in 5% (w/v) perfluoro-octanoic acid or 6 M guanidinium chloride, inserts spontaneously and folds qu
71 p, the protein is captured by a detergent as guanidinium chloride is diluted to a non-denaturing conc
73 ations to investigate the effect of urea and guanidinium chloride on the structure of the intrinsical
74 spectroscopic techniques to examine whether guanidinium chloride, one of the most commonly used prot
75 methyl ester, N-acetyl lysine methyl ester, guanidinium chloride, or KCl and one member of a series
77 uctural stability studies with the chaotrope guanidinium chloride revealed that there is moderate des
78 ion, the 1H-15N HSQC spectrum taken at 1.5 M guanidinium chloride reveals that only the Rd-apocyt b56
80 hat mitochondrial malate dehydrogenase in 3M guanidinium chloride shows little residual secondary str
81 interaction model we show that, in urea and guanidinium chloride solutions, unfolding of an unusuall
83 mass spectrometry, denaturing reactions with guanidinium chloride, stopped-flow methods measuring cys
85 ion between apo-CCT and tubulin diluted from guanidinium chloride, ten major, stable contacts between
86 lowing transfer from a buffer containing 5 m guanidinium chloride to a buffer containing 0.5 m guanid
88 At pH* 4.00 with D2O at 10 degrees C and 6 M guanidinium chloride, unfolding shows a single, slow kin
89 es for unfolding by elevated temperature and guanidinium chloride were measured for each of the four
90 dinium chloride to a buffer containing 0.5 m guanidinium chloride were studied by measuring the time-
91 ce spectroscopy in varying concentrations of guanidinium chloride were used to extrapolate unfolding
93 due to the favorable association of urea or guanidinium chloride with the backbone of all residues a