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Chaperones/“ heat-shock proteins”
interact with polypeptides during folding to ensure proper 3-D structure and use ATP energy to catalyze the proper folding of proteins
Alpha-crystallin
prevents aggregation of misfolded proteins by holding them in a partially folded state to help maintain lens transparency (prevent cataracts)
Disulfide bridge formation
helps with protein folding and structure
Phosphorylation
removes negative charge
Acetylation
removes positive charge
Protein Trafficking
process of moving proteins from the ER through the Golgi and beyond
Proteasome
large complex of proteins that typically degrades misfolded and short-lived proteins
Polymerase Chain Reaction (PCR)
method for the amplification of specific sequences of DNA from a large, complex source
Gel electrophoresis
uses the charged nature of macromolecules to move them in an electrical field with porous material allowing the molecules to be separated as smaller molecules tend to move more rapidly through a meshwork than larger molecules
Southern blotting
used to detect specific DNA fragments using a DNA probe
Northern blotting
used to detect specific RNA fragments using a DNA probe
Western blotting
used to detect specific proteins, antibodies to that protein are used since they will specifically bind to the protein of interest
Southwestern blot
used to detect whether a sample contains a protein that can bind to a specific DNA sequence using a gel