switchSENSE®
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List of protein hydrodynamic diameters DH

ProteinMolecular weightDH measured with
switchSENSE® (i)
Dh calculated from
PDB file (ii)
PDB codeStructure
anti-human Fab fragment050 kDa06.6 nm07.2 nm3WD5


anti-human IgG150 kDa12.7 nm11.2 nm1IGT


anti-IgG Affibody®014 kDa03.9 nm03.9 nm2B88


Carbonic
anhydrase I
029 kDa04.9 nm04.9 nm2CAB


CD64031 kDa06.7 nm05.7 nm4ZNE


EGFR071 kDa07.1 nm07.8 nm1NQL


Erythropoetin021 kDa04.7 nm04.6 nm1BUY


GFP-Trap® (nanobody)013 kDa03.9 nm03.9 nm3OGO


Glutathion-S-Transferase026 kDa04.7 nm04.8 nm1B8X


Glycosylceramidase056 kDa06.4 nm06.2 nm3RIL


Her2 (Met1-Thr652)070 kDa07.6 nm07.7 nm1N8Z


HIV Env protein500 kDa11.0 nm11.5 nm4NCO


Human serum albumin069 kDa04.2 nm-1AO6


IGF-1R206 kDa13.3 nm--
Neutravidin060 kDa07.4 nm06.1 nm1VYO


p38 kinase041.5 kDa05.0 nm05.8 nm1W84


Pim-1031.5 kDa05.2 nm05.2 nm3C4E


Protein kinase A040 kDa05.5 nm05.6 nm1Q8U


Pyruvate kinase M2058 kDa06.9 nm06.4 nm1T5A


Sting dimer056 kDa06.5 nm06.6 nm4F5D


Sting monomer028 kDa05.1 nm04.9 nm4F5E


TNFα017.5 kDa04.4 nm04.4 nm3WD5


Ubiquitin008.5 kDa03.2 nm03.4 nm1UBQ


(i) Experimental protein diameters are analyzed from switching dynamics measurements with standard 48 bp DNA nanolevers (length = 16 nm) using the drift-diffusion ‘Lollipop’ model described in J. Phys. Chem. B 118, 597 (2014).

(ii) Theoretical calculations of protein diameters from PDB files are performed with the HydroPro algorithm [Garcia de la Torre et al. Biophys. J. 78:179, (2000)], that calculates an effective hydrodynamic diameter from atomic coordinates using a hydrodynamic bead-shell model. Note that crystal structures may not always reflect the native protein structure in solution (especially for large proteins with several domains connected by flexible linkers).