Conserved Folding Pathways of α-Lactalbumin and Lysozyme Revealed by Kinetic CD, Fluorescence, NMR, and Interrupted Refolding Experiments

Schlepckow, Kai; Wirmer, Julia; Bachmann, Annett; Kiefhaber, Thomas; Schwalbe, Harald

doi:10.1016/j.jmb.2008.02.033

Cited by 27 publications

(31 citation statements)

References 69 publications

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“…91 Our interrupted-unfolding experiments, however, clearly showed that minor kinetic phases during GLA refolding were attributed to the slow isomerizations in the U and I states ( Supplementary Fig. S1 and Table S2); hence, the triangular-pathway model cannot be applied to the present results.…”

Section: Discussionmentioning

confidence: 69%

Different Folding Pathways Taken by Highly Homologous Proteins, Goat α-Lactalbumin and Canine Milk Lysozyme

Nakamura

Makabe

Tomoyori

et al. 2010

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 69%

Different Folding Pathways Taken by Highly Homologous Proteins, Goat α-Lactalbumin and Canine Milk Lysozyme

Nakamura

Makabe

Tomoyori

et al. 2010

Journal of Molecular Biology

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“…Time-resolved folding and unfolding of α-lactalbumin [22], [26], [27], [28], [29] and other proteins [30] have been studied by conventional 1D and 2D NMR. Data from these studies were evaluated by integrating individual peaks and fitting time constants locally or globally.…”

Section: Resultsmentioning

confidence: 99%

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

et al. 2010

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To obtain insight into the functions of proteins and their specific roles, it is important to establish efficient procedures for exploring the states that encapsulate their conformational space. Global Protein folding State mapping by multivariate NMR (GPS NMR) is a powerful high-throughput method that provides such an overview. GPS NMR exploits the unique ability of NMR to simultaneously record signals from individual hydrogen atoms in complex macromolecular systems and of multivariate analysis to describe spectral variations from these by a few variables for establishment of, and positioning in, protein-folding state maps. The method is fast, sensitive, and robust, and it works without isotope-labelling. The unique capabilities of GPS NMR to identify different folding states and to compare different unfolding processes are demonstrated by mapping of the equilibrium folding space of bovine α-lactalbumin in the presence of the anionic surfactant sodium dodecyl sulfate, SDS, and compare these with other surfactants, acid, denaturants and heat.

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“…Characterization of these structures and the factors involved in their stability would provide an insight to understand how and when various forces come into play in directing protein folding [1][2][3][4]. The development of a broad range of techniques has led to the identification and characterization of stable intermediates in several proteins [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Effect of polyethylene glycols on the alkaline-induced molten globule intermediate of bovine serum albumin

Wang

et al. 2012

International Journal of Biological Macromolecules

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Conserved Folding Pathways of α-Lactalbumin and Lysozyme Revealed by Kinetic CD, Fluorescence, NMR, and Interrupted Refolding Experiments

Cited by 27 publications

References 69 publications

Different Folding Pathways Taken by Highly Homologous Proteins, Goat α-Lactalbumin and Canine Milk Lysozyme

Different Folding Pathways Taken by Highly Homologous Proteins, Goat α-Lactalbumin and Canine Milk Lysozyme

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

Effect of polyethylene glycols on the alkaline-induced molten globule intermediate of bovine serum albumin

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