Protein folding and stability using denaturants (Q46927993)

26 December 2017

title

Protein folding and stability using denaturants (English)

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26 December 2017

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3

Doug Barrick

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26 December 2017

1

Timothy O Street

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26 December 2017

author name string

Naomi Courtemanche

series ordinal

2

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26 December 2017

publication date

1 January 2008

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26 December 2017

published in

Methods in Cell Biology

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26 December 2017

volume

84

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26 December 2017

page(s)

295-325

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26 December 2017

Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride.

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Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential inte

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Protein stability: functional dependence of denaturational Gibbs energy on urea concentration

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Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

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Measuring the stability of partly folded proteins using TMAO.

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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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3 The preparation of guanidine hydrochloride

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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Urea denaturation of barnase: pH dependence and characterization of the unfolded state

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Macromolecules and water: probing with osmotic stress

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Effect of salt on the urea-unfolded form of barstar probed by m value measurements

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THE EFFECT OF COMPOUNDS OF THE UREA-GUANIDINIUM CLASS ON THE ACTIVITY COEFFICIENT OF ACETYLTETRAGLYCINE ETHYL ESTER AND RELATED COMPOUNDS

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Natively disordered proteins: functions and predictions

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Revisiting volume changes in pressure-induced protein unfolding.

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Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding

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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

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Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation

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A Naturally Occurring Protective System in Urea-Rich Cells: Mechanism of Osmolyte Protection of Proteins against Urea Denaturation

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Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 1. Solution conformational and hydrodynamic properties

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Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves

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Structure and Notch receptor binding of the tandem WWE domain of Deltex

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10.1016/S0091-679X(07)84011-8

Identifiers

DOI

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26 December 2017

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26 December 2017