Supplementary Table. Molecular weight and electrophoretic mobility diameters (EMD) of protein complexes studied by GEMMA. The EMDs for the proteins in bold were determined in our laboratory. As indicated in the table, the molecular weights of these proteins were from the reference listed or determined by ESI or MALDI-MS. The EMDs and molecular weights for the proteins in plain text are from Bacher et al [1].

Peptide/Protein / No. Subunits / Molecular Weight (kDa) / Electrophoretic Moblity Diameter (nm) / Method of Mass Determination
Oxytocin / trimer / 3.02 / 2.6
Angiotensin I / trimer / 3.89 / 2.7
Insulin B-chain / monomer / 3.50 / 2.85
dimer / 6.99 / 3.4
trimer / 10.5 / 3.9
Insulin / monomer / 5.73 / 3.15
dimer / 11.5 / 3.9
trimer / 17.2 / 4.5
Ubiquitin / monomer / 8.57 / 3.6
dimer / 17.1 / 4.5
trimer / 25.7 / 5.2
Ferredoxin / monomer / 11.0 / 3.85
dimer / 22.0 / 4.8
Cytochrome c / monomer / 12.3 / 4.15
dimer / 24.6 / 5.15
trimer / 36.9 / 5.9
Ribonuclease A / monomer / 13.7 / 4.3
dimer / 27.4 / 5.4
tetramer / 54.7 / 6.7
Lysozyme / monomer / 14.3 / 4.3
dimer / 28.6 / 5.4
trimer / 42.9 / 6.15
Ribonuclease B / monomer / 14.8 / 4.4
dimer / 29.5 / 5.5
tetramer / 59.1 / 6.85
Myoglobin / monomer / 17.6 / 4.6
dimer / 35.1 / 5.7
trimer / 52.7 / 6.45
-Lactoglobulin A / monomer / 18.3 / 4.7
dimer / 36.6 / 5.8
trimer / 54.8 / 6.6
Trypsin / monomer / 23.9 / 5.3
dimer / 47.7 / 6.45
Apoferritin,Archaeoglobus fulgidus / monomer / 20.2 / 4.72 / ESI-MS of subunits
dimer / 40.4 / 5.87
tetramer / 80.8 / 7.46
tetraeicoamer / 484.4 / 13.1
Carbonic anhydrase II, bovine / monomer / 29 / 5.31 / MALDI-TOF-MS
dimer / 58 / 6.75
trimer / 87 / 7.71
Ecotin / monomer / 32.2 / 5.68 / ESI-MS of monomer and dimer
dimer / 64.4 / 7.08
trimer / 96.6 / 7.81
Fetuin / monomer / 43.4 / 6.2
dimer / 86.7 / 7.75
tetramer / 173.4 / 9.95
Albumin, hen egg / monomer / 44.6 / 6.3
dimer / 89.1 / 7.8
Enolase,Saccharomyces cerevisiae / monomer / 46.7 / 6.58 / ESI-MS of monomer, dimer, and tetramer
dimer / 93.3 / 8.40
trimer / 140.0 / 9.43
tetramer / 186.6 / 10.45
Streptavidin / tetramer / 52.2 / 6.54 / ESI-MS of tetramer
octamer / 104.4 / 8.43
Factor IX / monomer / 53.2 / 6.65
Avidin / tetramer / 64.0 / 6.9
octamer / 127.9 / 8.8
Hemoglobin, bovine / monomer / 64.7 / 6.9
dimer / 129.4 / 8.7
Hemoglobin, human / monomer / 65.0 / 6.9
dimer / 130.0 / 8.8
Albumin, bovine serum / monomer / 66.4 / 7.1
dimer / 132.8 / 9.0
trimer / 199.2 / 10.4
Albumin, human serum / monomer / 66.5 / 6.96 / MALDI-TOF-MS
dimer / 134 / 8.83
GroES / heptamer / 72.7 / 7.60 / ESI-MS of heptamer
tetradecamer / 145.4 / 9.56
holo-Transferrin / monomer / 78.4 / 7.6
dimer / 156.8 / 9.5
trimer / 235.1 / 10.9
Alcohol dehydrogenase, equine liver / dimer / 80.3 / 7.68 / Loo, 1995[2]
tetramer / 160 / 9.63
Acylase I / monomer / 90.5 / 8.0
-Galactosidase / monomer / 116.4 / 8.8
dimer / 232.7 / 11.1
trimer / 349.1 / 12.65
tetramer / 465.4 / 13.9
Alcohol Dehydrogenase,Saccharomyces cerevisiae / tetramer / 147.6 / 9.15 / ESI-MS
Ig G, bovine / monomer / 148.9 / 9.3
dimer / 297.7 / 11.7
trimer / 446.6 / 13.4
Ig G-peroxidase (conjugate) / monomer / 188.9 / 10.2
20S Proteasome,-ring, Methanosarcina thermophila / heptamer / 191.9 / 10.8 / Loo et al., 2005[3]
Catalase / tetramer / 233.0 / 10.8
octamer / 466.1 / 13.7
GroEL / heptamer / 400 / 13.1 / MALDI-TOF-MS of subunits
tetradecamer / 800 / 15.6
28-mer / 1600 / 20.3
Apoferritin, equine spleen / tetraeicosamer / 480 / 12.9 / MALDI-TOF-MS of subunits
48-mer / 960 / 16.9
Thyroglobulin / monomer / 660 / 14.9
20S Proteasome,Methanosarcina thermophila / 28-mer / 690.5 / 15.5 / Loo et al., 2005[3]
IgM / monomer / 960.5 / 17.4
dimer / 1921 / 21.65
CCMV / 180-mer/RNA / 4600 / 25.4 / Bancroft et al., 1968[4]
Vault, NT-MVP / 96-mer / 9300 / 36.1 / MALDI-TOF-MS of subunits
Vault, CP-MVP / 96-mer / 9400 / 37.5 / MALDI-TOF-MS of subunits
Vault, HT7-MVP / 96-mer / 9600 / 39.3 / MALDI-TOF-MS of subunits
Vault, GL-MVP / 96-mer / 11900 / 42.7 / MALDI-TOF-MS of subunits

References

1.Bacher, G.; Szymanski, W. W.; Kaufman, S. L.; Zollner, P.; Blaas, D.; Allmaier, G. Charge-Reduced Nano Electrospray Ionization Combined with Differential Mobility Analysis of Peptides, Proteins, Glycoproteins, Noncovalent Protein Complexes and Viruses. J. Mass Spectrom.2001, 36, 1038-1052.

2.Loo, J. A. Observation of Large Subunit Protein Complexes by Electrospray Ionization Mass Spectrometry. J. Mass Spectrom.1995, 30, 180-183.

3.Loo, J. A.; Berhane, B.; Kaddis, C. S.; Wooding, K. M.; Xie, Y.; Kaufman, S. L.; Chernushevich, I. V. Electrospray Ionization Mass Spectrometry and Ion Mobility Analysis of the 20S Proteasome Complex. J. Am. Soc. Mass Spectrom.2005, 16, 998-1008.

4.Bancroft, J. B.; Hiebert, E.; Rees, M. W.; Markham, R. Properties of Cowpea Chlorotic Mottle Virus, Its Protein and Nucleic Acid. Virology1968, 34, 224-239.