Native protein denaturation using urea | Zendy

Kyle K. Biggar | Zendy; Neal J. Dawson | Zendy; Kenneth B. Storey | Zendy

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Native protein denaturation using urea

Author(s) -

Kyle K. Biggar,

Neal J. Dawson,

Kenneth B. Storey

Publication year - 2017

Publication title -

biotechniques

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.617

H-Index - 131

eISSN - 1940-9818

pISSN - 0736-6205

DOI - 10.2144/000114501

Subject(s) - denaturation (fissile materials) , cooperativity , kinetics , chemistry , urea , protein stability , protein folding , biophysics , biochemistry , biology , physics , nuclear chemistry , quantum mechanics

Protocol Summary Here we present a new protocol to analyze protein unfolding kinetics using a quantified real-time thermocycler. This technique enables the analysis of a wide range of denaturants (and their interactions with temperature change) on protein stability in a multi-well platform, where samples can be run in parallel under virtually identical conditions and with highly sensitive detection. Using this set-up, researchers can evaluate the half-maximal rate of protein denaturation (Knd), maximum rate of denaturation (Dmax), and the cooperativity of individual denaturants in protein unfolding (µ-coefficient).

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