Table 1.

Gel shifts of various helical membrane proteins on SDS-PAGE

Protein*MW (kDa)Gel shift dMW, %Ref.
App.Formula
I. tartaricus F-type ATPase c subunit41
    Undecamer5397−46
    Monomer6.58.8−26
Archaeal ammonium transporter Amt-142
    Trimer90134−33
    Monomer3345−27
E. coli lactose permease3347−3043
Vitamin B12 transporter BtuC2635−2644
H+/Cl exchange transporter ClC3851−2545
Potassium channel KcsA tetramer6076−2146
Phospholamban47
    Pentamer2930−17
    Monomer96.1+48
Particulate methane monooxygenase48
    pmoA subunit2428−14
    pmoB subunit47462
    pmoC subunit2230−27
Glycerol facilitator channel GlpF2934−1549
E. coli MscS channel50
    Dimer5262−16
    Monomer2731−12
Multidrug transporter AcrB100115−1351
Glycerol-3-phosphate transporter GlpT4550−1052
Spinach aquaporin3132−353
Rhomboid family protease GlpG3131054
M. tuberculosis MscL channel monomer2016+2655
β2-adrenergic receptor6247+3056
M. thermoautotrophicum MthK tetramer200149+3457
  • *Proteins were selected from a list of non-redundant helical membrane proteins based on the availability of published SDS-PAGE data and are arranged in approximate order of faster-to-slower than expected migration rates. The helical nature of each protein has been confirmed in a high-resolution structure. Oligomeric data were obtained only from gels where extrinsic cross-linking agents were absent.

  • The migration distances of proteins on SDS-PAGE gels reported in the papers examined, compared to standards on these gels. dMW = (apparent MW − formula MW)/formula MW × 100%. Negative dMWs indicate movement faster (at a lower apparent MW) than expected and vice-versa.