Thermodynamic and kinetic characterization of apoHmpH, a fast-folding bacterial globin

Journal of Molecular Biology
Ye-Jin EunSilvia Cavagnero

Abstract

Despite the widespread presence of the globin fold in most living organisms, only eukaryotic globins have been employed as model proteins in folding/stability studies so far. This work introduces the first thermodynamic and kinetic characterization of a prokaryotic globin, that is, the apo form of the heme-binding domain of flavohemoglobin (apoHmpH) from Escherichia coli. This bacterial globin has a widely different sequence but nearly identical structure to its eukaryotic analogues. We show that apoHmpH is a well-folded monomeric protein with moderate stability at room temperature [apparent Delta G degrees (UN(w))=-3.1+/-0.3 kcal mol(-1); m(UN)=-1.7 kcal mol(-1) M(-1)] and predominant alpha-helical structure. Remarkably, apoHmpH is the fastest-folding globin known to date, as it refolds about 4- to 16-fold more rapidly than its eukaryotic analogues (e.g., sperm whale apomyoglobin and soybean apoleghemoglobin), populating a compact kinetic intermediate (beta(I)=0.9+/-0.2) with significant helical content. Additionally, the single Trp120 (located in the native H helix) becomes locked into a fully native-like environment within 6 ms, suggesting that this residue and its closest spatial neighbors complete their folding at ultrafas...Continue Reading

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Citations

May 26, 2009·The Journal of Physical Chemistry. B·Ashok Sekhar, Silvia Cavagnero
May 16, 2009·Advances in Colloid and Interface Science·L Muthuselvi, Aruna Dhathathreyan
May 28, 2020·The Journal of Physical Chemistry. B·Rayna M AddabboSilvia Cavagnero
Apr 20, 2010·Analytical Chemistry·David R ZiehrSilvia Cavagnero
Jun 12, 2013·The Journal of Physical Chemistry. B·Li ZhuSilvia Cavagnero
Jul 14, 2018·The Journal of Physical Chemistry. B·Angela E VarelaSilvia Cavagnero
Aug 6, 2010·Methods : a Companion to Methods in Enzymology·Sarah A WeinreisSilvia Cavagnero

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