Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding
Author:
Publisher
Springer New York
Link
http://link.springer.com/content/pdf/10.1007/978-1-4939-8820-4_19
Reference3 articles.
1. Lea WA, O'Neil PT, Machen AJ, Naik S, Chaudhri T, McGinn-Straub W, Tischer A, Auton MT, Burns JR, Baldwin MR, Khar KR, Karanicolas J, Fisher MT (2016) Chaperonin-based biolayer interferometry to assess the kinetic stability of metastable, aggregation-prone proteins. Biochemistry 55(35):4885–4908. https://doi.org/10.1021/acs.biochem.6b00293
2. Pastor A, Singh AK, Fisher MT, Chaudhuri TK (2016) Protein folding on biosensor tips: folding of maltodextrin glucosidase monitored by its interactions with GroEL. FEBS J 283(16):3103–3114. https://doi.org/10.1111/febs.13796
3. Friedler A, Hansson LO, Veprintsev DB, Freund SM, Rippin TM, Nikolova PV, Proctor MR, Rudiger S, Fersht AR (2002) A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc Natl Acad Sci U S A 99(2):937–942. https://doi.org/10.1073/pnas.241629998
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