Observing picomolar protein unfolding using resonance light scattering

Alain Alvarez Bolano*, Kristian B. Arvesen, Kasper F. Hjuler, Peter Bjerring, Steffen B. Petersen

*Kontaktforfatter

Publikation: Working paper/PreprintPreprint

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Abstract

We here present a novel and sensitive methodology for determining the melting point (MP) of Bovine Serum Albumin (BSA) from micromolar to picomolar concentration levels under label free conditions. At 1 pM we could model the melting with a sharp gaussian. However, from the transient state observed during the melting process by using a simple exponential decay model we determined a time constant of 67 seconds. We applied this methodology by studying a 3.3 pM sample of a botulinum toxin A (BoNT-A) (stabilized with 2.8 nanomolar denatured Human Serum Albumin (HSA)). We were able to determine the Tm of BoNT-A in the presence of the approximately 1000-fold more concentrated HSA.
OriginalsprogEngelsk
UdgiverbioRxiv
Antal sider8
DOI
StatusUdgivet - 22 nov. 2024

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