Molten Globule of Cytochrome c Studied by Small Angle X-ray Scattering

Kataoka, Mikio; Hagihara, Yoshihisa; Mihara, Kenichi; Goto, Yuji

doi:10.1006/jmbi.1993.1064

Cited by 237 publications

(210 citation statements)

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“…4C). Therefore, we formers (Ohgushi & Wada, 1983;Goto et al, 1990aGoto et al, , 1990bJeng conclude that the number of basis components is two for SI and & Englander, 1991; Kataoka et al, 1993;Bychkova et al, 1996; S,, while three for S,. Kamatari et al, 1996).…”

Section: Minimum Number Of Basis Componentsmentioning

confidence: 85%

Conformational diversity of acid‐denatured cytochrome c studied by a matrix analysis of far‐UV CD spectra

Konno

1998

Protein Science

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The singular value decomposition (SVD) analysis was applied to a large set of far-ultraviolet circular dichroism (far-UV CD) spectra (100-400 spectra) of horse heart cytochrome c (cyt c). The spectra were collected at pH 1.7-5.0 in (NH4)2S04r sorbitol and 2,2,2-trifluoroethanol (TFE) solutions. The present purpose is to develop a rigorous matrix method applied to far-UV CD spectra to resolve in details conformational properties of proteins in the non-native (or denatured) regions. The analysis established that three basis spectral components are contained in a data set of difference spectra (referred to the spectrum of the native state) used here. By a further matrix transformation, any observed spectrum could be decomposed into fractions of the native (N), the molten-globule (MG), the highly denatured (D), and the alcohol-induced helical (H) spectral forms. This method could determine fractional transition curves of each conformer as a function of solution conditions, which gave the results consistent with denaturation curves of cyt c monitored by other spectroscopic methods. The results in sorbitol solutions, for example, suggested that the preferential hydration effect of the co-solvent stabilizes the MG conformer of cyt c. This report has found that the systematic SVD analysis of the far-UV CD spectra is a powerful tool for the conformational analysis of the non-native species of a protein when it is suitably supplemented with other experimental methods.

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Section: Minimum Number Of Basis Componentsmentioning

confidence: 85%

Conformational diversity of acid‐denatured cytochrome c studied by a matrix analysis of far‐UV CD spectra

Konno

1998

Protein Science

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“…It gives a clear peak for the globular conformation, while it shows a plateau and then increases monotonically for the unfolded chain-like conformer (Flanagan et al, 1993;Kataoka et al, 1993;Kataoka & Goto, 1996). Figure 8 shows the Kratky plots for the three typical conformational states of lysozyme, N, H, and U.…”

Section: Chain Conformations In Methanovwater As Monitored By Small-amentioning

confidence: 99%

The methanol‐induced transition and the expanded helical conformation in hen lysozyme

et al. 1998

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Methanol-induced conformational transitions of hen egg white lysozyme were investigated with a combined use of farand near-UV CD and N M R spectroscopies, ANS binding and small-angle X-ray scattering. Addition of methanol induced no global change in the native conformation itself, but induced a transition from the native state to the denatured state which was highly cooperative, as shown by the coincidence of transition curves monitored by the far-and near-UV CD spectroscopy, by isodichroic points in the far-and near-UV CD spectra and by the concomitant disappearance of individual 'H N M R signals of the native state. The ANS binding experiments could detect no intermediate conformer similar to the molten globule state in the process of the methanol denaturation. However, at high concentration of methanol, e.g., 60% (v/v) methanol/water, a highly helical state (H) was realized. The H state had a helical content much higher than the native state, monitored by far-W CD spectroscopy, and had no specific tertiary structure, monitored both by near-UV CD and N M R spectroscopy. The radius of gyration in the H state, 24.9 A, was significantly larger than that in the native state (15.7 A). The Kratky plot for the H state did not show a clear peak and was quite similar to that for the urea-denatured state, indicating a complete lack of globularity. Thus we conclude that the H state has a considerably expanded, flexible broken rod-like conformation which is clearly distinguishable from the "molten globule" state. The stability of both N and H states depends on pH and methanol concentration. Thus a phase diagram involving N and H was constructed.

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“…In general, the scattering curve for a globular conformation follows Porod's law, I(q) / q À4 in the large-q region, whereas the scattering profile from an expanded unfolding conformation is proportional to q À2 at moderate q, and is then proportional to q À1 at small q values (Glatter, 1982;Flanagan et al, 1992;Kataoka et al, 1993Kataoka et al, , 1995. Furthermore, the Kratky plot of the scattering curve for the globular structure shows a clear peak, whereas that of a molten globule has a plateau and then increases gradually with q (Glatter, 1982;Flanagan et al, 1992;Kataoka et al, 1993Kataoka et al, , 1995.…”

Section: Saxs Analysis Of Rseas and Their Complexes With Rsebmentioning

confidence: 99%

“…Furthermore, the Kratky plot of the scattering curve for the globular structure shows a clear peak, whereas that of a molten globule has a plateau and then increases gradually with q (Glatter, 1982;Flanagan et al, 1992;Kataoka et al, 1993Kataoka et al, , 1995. Thus, Kratky analysis was further carried out for the measured SAXS data in order to obtain more useful information on the folding status.…”

Section: Saxs Analysis Of Rseas and Their Complexes With Rsebmentioning

confidence: 99%

Solution structures of RseA and its complex with RseB

Jin

Kim

Rho

et al. 2008

J Synchrotron Radiat

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The bacterial envelope stress response, which is responsible for sensing stress signals in the envelope and for turning on the E -dependent transcription, is modulated by the binding of RseB to RseA. In this study, the solution structures of RseA and its complex with RseB were analyzed using circular dichroism and small-angle X-ray scattering. The periplasmic domain of RseA is unstructured and flexible when it is not bound to RseB. However, upon the formation of the stable complex with RseB, RseA induces conformational changes in RseB and, at the same time, RseA becomes more structured. Furthermore, it appears that some other undefined region of RseA, as well as the previously identified minimum region (amino acid 169-186), is also involved in RseB binding. It is thought that these conformational changes are relevant to the proteolytic cleavage of RseA and the modulation of envelope stress response.

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Molten Globule of Cytochrome c Studied by Small Angle X-ray Scattering

Cited by 237 publications

References 0 publications

Conformational diversity of acid‐denatured cytochrome c studied by a matrix analysis of far‐UV CD spectra

Conformational diversity of acid‐denatured cytochrome c studied by a matrix analysis of far‐UV CD spectra

The methanol‐induced transition and the expanded helical conformation in hen lysozyme

Solution structures of RseA and its complex with RseB

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