3) You are studying a protein that you think consists of a heterodimer composed of a 30 kDa and a 40 kDa subunit, which are joined together by disulphide bonds. In addition to your protein sample you have available a SDS-PAGE gel, an electrophesis apparatus like the one you used in the laboratory, and a Bio-Rad Precision Protein Kaleidoscope standard (Bio-Rad catalogue number 161-0375). You also have access to two different sample buffers. Buffer A contains 4% (v/v) SDS and 5% (v/v) Ã-mercapto ethanol. Buffer B contains 4% (v/v) SDS but no Ã-mercapto ethanol. As per the practical, samples are heated at 95oC for 4 minues before they are loaded onto an SDS-PAGE gel and electrophoresed.
Describe the experimental methods that would allow you to test your hypothesis. Provide sufficient detail such that an interested reader could faithfully repeat your experiment. In your answer describe the chemistry and biochemistry involved in your treatment.
(You determine hypothesis)
3) You are studying a protein that you think consists of a heterodimer composed of a 30 kDa and a 40 kDa subunit, which are joined together by disulphide bonds. In addition to your protein sample you have available a SDS-PAGE gel, an electrophesis apparatus like the one you used in the laboratory, and a Bio-Rad Precision Protein Kaleidoscope standard (Bio-Rad catalogue number 161-0375). You also have access to two different sample buffers. Buffer A contains 4% (v/v) SDS and 5% (v/v) Ã-mercapto ethanol. Buffer B contains 4% (v/v) SDS but no Ã-mercapto ethanol. As per the practical, samples are heated at 95oC for 4 minues before they are loaded onto an SDS-PAGE gel and electrophoresed.
Describe the experimental methods that would allow you to test your hypothesis. Provide sufficient detail such that an interested reader could faithfully repeat your experiment. In your answer describe the chemistry and biochemistry involved in your treatment.
(You determine hypothesis)
