Protein Separation and PTMs Quiz

A method using dye to visualize proteins separated on a gel, often used for quick and affordable analysis.

A technique used to detect and identify specific proteins in a complex mixture. It involves transferring proteins from a gel to a membrane, followed by the use of antibodies to target specific proteins.

The process of separating proteins by size and charge using an electric field in a gel matrix.

This step in Western blotting prevents non-specific binding of antibodies to the membrane by blocking any unoccupied binding sites.

The step in Western blotting, where a labeled antibody binds to the target protein, allowing for visualization.

A technique used to separate, identify, and purify compounds based on various properties, such as size, charge, and binding specificity.

A purification technique that utilizes a stationary phase with immobilized substrate (ligand) to bind specific target molecules.

A stationary phase where the substrate is bound covalently, exposing reactive groups for binding.

A technique that utilizes charged resins (cationic or anionic) to separate proteins based on their charge.

Resins with negatively charged groups attracting positively charged cations.

Resins possessing positively charged groups attracting negatively charged anion.

Elution process involves increasing the ionic strength or changing the pH of the buffer to release bound proteins.

A method useful for purifying proteins with well-defined charge, often used as an intermediate purification step.

A method of cell lysis that involves repeated cycles of freezing and thawing, causing ice crystal formation that disrupts cell membranes.

A method of cell lysis that uses detergents to disrupt the lipid bilayers of cell membranes, making them soluble in solution.

A method of cell lysis that uses organic solvents to precipitate proteins and disrupt cell membranes.

A method of cell lysis that disrupts the hydrogen bonding network in proteins using chaotropic agents, making them soluble.

A protein purification technique that separates components based on their density by spinning samples at high speeds.

A protein purification technique that involves altering the solubility of proteins to cause them to aggregate and precipitate out of solution.

A method of protein precipitation using salts like ammonium sulphate to alter protein solubility.

A method of protein precipitation using organic solvents or changes in pH.

The complete set of proteins expressed by a genome, cell, tissue, or organism.

Chemical modifications that occur to a protein after translation, often altering its function, localization, or stability.

The study of the proteome, including the identification, quantification, and characterization of proteins, as well as their interactions and functions.

The process of separating proteins based on their physical or chemical properties, such as size, charge, or affinity for specific molecules.

The process of identifying the specific type of protein present in a sample, using techniques like mass spectrometry.

The study of all RNA molecules in a cell or organism, including messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA).

The process of converting genetic information from DNA to RNA.

The process of synthesizing proteins from mRNA.

Understanding where a protein is located within a cell or organism, which determines its function.

Analyzing the changes made to a protein after it's been made, like adding a tag or changing its shape.

Investigating the biological roles of individual proteins, groups of proteins, or entire protein networks.

Studying the three-dimensional structure of proteins to understand their function and potential for drug development.

Analyzing how proteins interact with each other, including which proteins interact and where.

Methods for studying proteins, categorized as low-throughput (individual studies) and high-throughput (mass spectrometry-based for large-scale analysis).

This technique separates proteins based on their size by passing them through a gel matrix containing polyacrylamide. The gel is treated with SDS (Sodium Dodecyl Sulfate), which denatures the proteins and gives them a uniform negative charge, allowing separation based on size alone.

Native PAGE uses an electric current to separate proteins based on their native charge and shape, without denaturation. This means it preserves the protein's original structure and allows analysis of its natural function.

This method separates proteins in two dimensions: first by their isoelectric point (pI) using isoelectric focusing (IEF), and second by their molecular weight using SDS-PAGE.

It's a modified form of 2DE that uses different fluorescent dyes to label and compare multiple protein samples on a single gel.

Blue native PAGE (BN-PAGE) is a technique that separates proteins in their native, functional state, allowing the study of protein assemblies or complexes.

Polyacrylamide is a polymer used to make gels for protein separation. It forms a porous matrix through which proteins migrate, allowing separation based on size and charge.

A synthetic linear polymer used in polyacrylamide gels, it is water-soluble and common in pulp and papermaking.

SDS breaks disulfide bonds in proteins and gives them a uniform negative charge, which helps in maintaining the charge-to-mass ratio during electrophoresis.