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© Research
Publication : Analytical biochemistry

Low-cost equilibrium unfolding of heme proteins using 2 μl samples

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Analytical biochemistry - 01 Dec 2013

Guca E, Roumestand C, Vallone B, Royer CA, Dellarole M

Link to Pubmed [PMID] – 23958270

Anal. Biochem. 2013 Dec;443(1):13-5

Equilibrium unfolding experiments provide access to protein thermodynamic stability revealing basic aspects of protein structure-function relationships. A limitation of these experiments stands on the availability of large amounts of protein samples. Here we present the use of the NanoDrop for monitoring guanidinium chloride-induced unfolding by Soret absorbance of monomeric heme proteins. Unfolding experiments using 2 μl of reactant are validated by fluorescence and circular dichroism spectroscopy and supported with five heme proteins including neuroglobin, cytochrome b5, and cyanoglobin. This work guarantees 2 orders of magnitude reduction in protein expense. Promising low-cost protein unfolding experiments following other chromophores and high-throughput screenings are discussed.

http://www.ncbi.nlm.nih.gov/pubmed/23958270