(Q43503107)

24 November 2017

title

The contribution of a covalently bound cofactor to the folding and thermodynamic stability of an integral membrane protein (English)

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24 November 2017

The Contribution of a Covalently Bound Cofactor to the Folding and Thermodynamic Stability of an Integral Membrane Protein (English)

1 reference

https://api.crossref.org/works/10.1016/J.JMB.2010.09.003

15 July 2024

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24 November 2017

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Paula J Booth

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24 November 2017

language of work or name

English

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publication date

17 September 2010

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full work available at URL

24 November 2017

https://api.elsevier.com/content/article/PII:S0022283610009514?httpAccept=text/xml

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https://api.crossref.org/works/10.1016/J.JMB.2010.09.003

https://api.elsevier.com/content/article/PII:S0022283610009514?httpAccept=text/plain

15 July 2024

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https://api.crossref.org/works/10.1016/J.JMB.2010.09.003

Journal of Molecular Biology

15 July 2024

published in

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24 November 2017

volume

403

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24 November 2017

issue

4

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24 November 2017

page(s)

630-642

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Role of cofactors in metalloprotein folding

24 November 2017

cites work

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How do cofactors modulate protein folding?

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Role of cofactors in protein folding

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Nature of forces stabilizing the transmembrane protein bacteriorhodopsin in purple membrane

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Retinal Binding during Folding and Assembly of the Membrane Protein Bacteriorhodopsin†

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Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding

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Side-chain contributions to membrane protein structure and stability

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Folding scene investigation: membrane proteins

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Intermediates in the folding of the membrane protein bacteriorhodopsin

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Slow α Helix Formation during Folding of a Membrane Protein†

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The transition state for integral membrane protein folding

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Single-molecule FRET reveals sugar-induced conformational dynamics in LacY.

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Estimation of helix-helix association free energy from partial unfolding of bacterioopsin

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The role of retinal in the thermal stability of the purple membrane

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Analysis of folding and unfolding reactions of cytochrome b5

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Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements

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Membrane protein folding: beyond the two stage model.

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15 July 2024

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Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: demonstration of an apo-membrane.

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Structure and thermal stability of monomeric bacteriorhodopsin in mixed phospholipid/detergent micelles

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Using micellar mole fractions to assess membrane protein stability in mixed micelles

15 July 2024

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The analysis of protein folding kinetic data produced in protein engineering experiments

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15 July 2024

Identifiers

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24 November 2017

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