1993
DOI: 10.1021/bi00095a017 View full text |Buy / Rent full text
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Abstract: Whereas the salt-dependent conformational transition of acid-denatured horse ferricytochrome c at pH 2 is approximated by a two-state mechanism from the acid-unfolded state to the molten globule state [Kataoka, M., Hagihara, Y., Mihara, K., & Goto, Y. (1993) J. Mol. Biol. 229, 591-596], the corresponding transition in D2O has been proposed to involve a noncompact, alpha-helical intermediate state (the pre-molten globule state) [Jeng, M.-F., & Englander, S. W. (1991) J. Mol. Biol. 221, 1045-1061]. To examine th… Show more

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“…These results suggest that CSI is more suited to the preservation of solution-phase conformations than either the ESI or nanoESI methods. It is noted that the relative amount of folded cytochrome c characterized using CSI-MS at 10°C is consistent with that obtained by spectroscopic techniques [52]. Thus, a spray temperature of 10°C was adopted in this study.…”
Section: Resultssupporting
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“…These results suggest that CSI is more suited to the preservation of solution-phase conformations than either the ESI or nanoESI methods. It is noted that the relative amount of folded cytochrome c characterized using CSI-MS at 10°C is consistent with that obtained by spectroscopic techniques [52]. Thus, a spray temperature of 10°C was adopted in this study.…”
Section: Resultssupporting
“…Figure 3b shows the relative amount of folded cytochrome c in CSI mass spectra at solution pH values from 2.0 to 3.0 according to eq 1. As illustrated in Figure 3b, the relative amount of the folded form obtained by CSI-MS matches the values obtained using tryptophan fluorescence spectrometry [52]. These results indicate that the CSI-MS method preserves the native protein structure, especially under low pH values, and has the advantage of being able to accurately characterize acid-induced equilibrium unfolding transitions.…”
Section: Resultssupporting
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“…Goto (in prep., reproduced with permission) show the content of a-helix estimated by CD increases with chain compactness (see also Nishii et al, 1994 (Lattman et al, 1994), experiments by Goto et al (1993) were unable to confirm the observations of Jeng and Englander. The perspective described above is that secondary structures develop as an indirect consequence of hydrophobic collapse, due to steric and compactness constraints.…”
Section: Compactness In Chain Molecules Stabilizes Secondary Structuresmentioning
“…Bovine cytochrome c is a globular protein containing 104 amino acids (23 basic and 12 acidic amino acids) and one covalently attached heme group [64]. The unfolding of cytochrome c has been studied in solution [65] and using the vapor introduction technique described here [43,44]. Ubiquitin is a smaller protein with 12 basic and 11 acidic residues [66].…”
Section: Cytochrome C and Ubiquitin: Positive Polaritymentioning