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Ion Exchange Chromatography
Separate anion and cation
Anion Exchange
Attract negative charged ion
Cation Exchange
Attract positive charge ion
Hydrophobic Interaction Chromatography
Separate molecules based on hydrophobicity
Gel Filtration Chromatography
Molecules separated by size and shape
Affinity Chromatography
Ligand binds to specific molecule of interest
Immunoaffinity Chromatography
ligand binds to molecule but process can be reversed
Metal Chelate
Binding to metal-ion
Polyacrylamide Gel Electrophoresis
Separation based on size, shape and charge
SDS-PAGE
Separates by molecular mass forgetting charge
Ultracentrifugation
Separates molecules by mass, density and shape
Beta-alpha-beta motif
alpha helix connects two parallel strands of a beta sheet
Beta Hairpin
Antiparallel strands connected by relatively tight reverse turns
Alpha-Alpha Motif
Two successive antiparallel alpha helices pack against each other with their axes inclined
Greek Key Motif
Beta hairpin is folded over to form a 4-stranded antiparallel beta sheet
Supersecondary Structure
Specific, recognizable combinations of secondary structures
Iodoacetate
An alkylating agent that reacts with Cys residues
2-mercaptoethanol
A reducing agent that carries out reductive cleavage of disulfide bonds
Dansyl Chloride & Phenylisothiocyanate
A reagent used to identify N-terminal residues
Cyanogen bromide
A reagent that cleaves polypeptides into smaller fragments
Phenylisothiocyanate
A reagent used in sequencing polypeptides from the N-terminus
False
X-ray crystallography can be used to study proteins in their native cellular environment
True
Unit cell in a crystal refers to the smallest repeating unit of crystal lattice
False
In Cryo-EM, samples are frozen in crystalline ice matrix
True
NMR spectroscopy can be used to study protein dynamics, while x-ray crystallography provides a static snapshot of the protein structure
True
One advantage of Cryo-EM is that it does not require crystallization of the protein