Protein Purification and Proteomics

What this page covers

This unit sits in the Biochemical and Molecular Methods strand of Biochemistry. It follows a protein from sample to identification. The resources were made by GoConqr users, so styles vary, and that is useful when one explanation does not click.

• Separation and purification: the flashcards in Protein Separation Part 1 cover properties of proteins for purification, salting out, isoelectric point and isoelectric precipitation. Mind maps on chromatography, affinity chromatography and electrophoresis go with them.
• Measuring protein: separate mind maps cover UV absorption, the Lowry method, the BCA assay and the Bradford method.
• Identification: flashcards on mass spectrometry cover peptide mass fingerprinting, bottom-up and top-down identification, and labeling methods.
• Structure: a mind map on NMR and flashcards on protein crystallisation and X-ray data collection.

Where to start

Begin with the mind map Protein Purification, then open Protein Purification Methods. They give you the overall order of steps. Next, work through the flashcards in Protein Separation Part 1 and Biochemical Techniques for Protein Purification, which includes the Edman degradation cycle.

Using quizzes and maps together

Read a mind map first, then test yourself. The quiz Lab 3 | SDS PAGE fits after the electrophoresis maps. The quiz Proteomics suits the end of your study session. Note which questions you miss, then return to the matching map or flashcard deck.

Moving on to proteomics

Once purification feels familiar, move to the proteomics maps and the Protein Mass Spectroscopy Part 3 and Part 4 flashcards. The flowchart on the application of proteomics to nutrition research shows how the methods are used in practice.

Make it your own

Teachers can pull a mind map or deck straight into a lesson plan. Students can pick one method, such as the Bradford method, and write a few flashcards of their own to check what they remember.