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Quantifying the Kinetic Stability of Hyperstable Proteins via Time-Dependent SDS Trapping

https://doi.org/10.1021/bi201362z

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What this work says

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Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases

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Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels

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Protein kinetic stability

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Proteolytic Scanning Calorimetry: A Novel Methodology that Probes the Fundamental Features of Protein Kinetic Stability

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Protein Folding Studied Using Hydrogen-Exchange Labeling and Two-Dimensional NMR

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The Stability of Globular Protein

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Destabilisation of the structure of transthyretin is driven by Ca2+

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Deep blue autofluorescence reveals the instability of human transthyretin

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Molecular Switch between Structural Compaction and Thermodynamic Stability by the Xxx–Pro Interface in Transmembrane β-Barrels

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Kinetic Stability of Proteins in Beans and Peas: Implications for Protein Digestibility, Seed Germination, and Plant Adaptation

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Transthyretin as both a Sensor and a Scavenger of β-Amyloid Oligomers

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Designed protein reveals structural determinants of extreme kinetic stability

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Conservation of kinetic stability, but not the unfolding mechanism, between human transthyretin and a transthyretin-related enzyme

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Transthyretin can denature by an alternative pathway

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Physiological IgM Class Catalytic Antibodies Selective for Transthyretin Amyloid

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The Impact of Sodium Dodecyl Sulfate and 2-Mercaptoethanol on Antibody and Antigen Binding

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Transthyretin variants with improved inhibition of β-amyloid aggregation

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Susceptibility of Cu(I) transport ATPases to sodium dodecyl sulfate. Relevance of the composition of the micellar phase

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Globular Protein Folding In Vitro and In Vivo

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