Pressure Denaturation of Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus

Roitel, Olivier; Bec, Nicole; Lange, Reinhard; Balny, Claude; Branlant, Guy

doi:10.1006/bbrc.2001.4779

Cited by 9 publications

(4 citation statements)

References 26 publications

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“…This means that the transition observed for GdmCl denaturation corresponds to unfolding, with dissociation occurring silently within the unfolded baseline region. This therefore indicates that unlike many oligomeric proteins (15,26,28,29), high pressure does not induce dissociation of the Ure2 dimer, nor does it induce population of partially-folded intermediates under these experimental conditions. This study suggests that other methods that cause marginal destabilization of Ure2, such as urea (2) or pH (12), could be combined with hydrostatic pressure and thus might provide a useful means of investigating partially folded intermediates of Ure2.…”

Section: Unfolding Of Ure2 By a Combination Of High Pressure And Gdmclmentioning

confidence: 80%

Pressure Denaturation of the Yeast Prion Protein Ure2

Zhou

Zhu

Balny

et al. 2001

Biochemical and Biophysical Research Communications

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Section: Unfolding Of Ure2 By a Combination Of High Pressure And Gdmclmentioning

confidence: 80%

Pressure Denaturation of the Yeast Prion Protein Ure2

Zhou

Zhu

Balny

et al. 2001

Biochemical and Biophysical Research Communications

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“…In contrast to the use of temperature or chemical compounds to modify the protein structure, high pressure has almost no effect on the free energy of the system, nor does it depend on the equilibrium with denaturant from the medium [18]. Several recent studies have pointed out the advantages of high pressure to probe and analyse the structural stability of a number of different proteins [19–24].…”

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confidence: 99%

Imagination can create false autobiographical memories

Mazzoni¹,

Memon²

2003

Psychological Science

197

156

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Previous studies have shown that imagining an event can alter autobiographical beliefs. The current study examined whether it can also create false memories. One group of participants imagined a relatively frequent event and received information about an event that never occurs. A second group imagined the nonoccurring event and received information about the frequent event. One week before and again 1 week immediately after the manipulation, participants rated the likelihood that they had experienced each of the two critical events and a series of noncritical events, using the Life Events Inventory. During the last phase, participants were also asked to describe any memories they had for the events. For both events, imagination increased the number of memories reported, as well as beliefs about experiencing the event. These results indicate that imagination can induce false autobiographical memories.

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“…These works have shown that high hydrostatic pressure can modify the structure or the function of enzymes by altering intra‐ or intermolecular interactions involved in protein stability [13,14]. However, relatively few studies have been performed to correlate conformational modifications of an enzyme to changes in its catalytic activity; although it is generally recognized that conformational integrity is important for preserving the activity of an enzyme [15–17].…”

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confidence: 99%

Fluorescence and FTIR study of pressure‐induced structural modifications of horse liver alcohol dehydrogenase (HLADH)

Trovaslet

Dallet‐Choisy

Meersman

et al. 2002

European Journal of Biochemistry

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The process of pressure-induced modification of horse liver alcohol dehydrogenase (HLADH) was followed by measuring in situ catalytic activity (up to 250 MPa), intrinsic fluorescence (0.1-600 MPa) and modifications of FTIR spectra (up to 1000 MPa). The tryptophan fluorescence measurements and the kinetic data indicated that the pressure-induced denaturation of HLADH was a process involving several transitions and that the observed transient states have characteristic properties of molten globules. Low pressure (< 100 MPa) induced no important modification in the catalytic efficiency of the enzyme and slight conformational changes, characterized by a small decrease in the centre of spectral mass of the enzyme's intrinsic fluorescence: a native-like state was assumed. Higher pressures (100-400 MPa) induced a strong decrease of HLADH catalytic efficiency and further conformational changes. At 400 MPa, a dimeric molten globule-like state was proposed. Further increase of pressure (400-600 MPa) seemed to induce the dissociation of the dimer leading to a transition from the first dimeric molten globule state to a second monomeric molten globule. The existence of two independent structural domains in HLADH was assumed to explain this transition: these domains were supposed to have different stabilities against high pressure-induced denaturation. FTIR spectroscopy was used to follow the changes in HLADH secondary structures. This technique confirmed that the intermediate states have a low degree of unfolding and that no completely denatured form seemed to be reached, even up to 1000 MPa.

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Pressure Denaturation of Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus

Cited by 9 publications

References 26 publications

Pressure Denaturation of the Yeast Prion Protein Ure2

Pressure Denaturation of the Yeast Prion Protein Ure2

Imagination can create false autobiographical memories

Fluorescence and FTIR study of pressure‐induced structural modifications of horse liver alcohol dehydrogenase (HLADH)

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