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You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.

You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.

Biology (MindTap Course List)
Biology (MindTap Course List)
11th Edition
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Chapter3: The Chemistry Of Life: Organic Compounds
Section: Chapter Questions
Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...
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You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.
Transcribed Image Text:You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.
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