Biomolecules and Metabolism - Proteins Structure Analysis

These flashcards cover key terms and definitions related to protein structure analysis and methods of protein purification studied in the lecture.

Protein Domain

Independently folding, stable structural units within a protein, usually about 50-250 amino acids long.

Structural Role

Provides a stable framework for a protein’s overall architecture.

Functional Role

Allows each domain to have a specific job and work together for complex functions.

Topological Domains

Regions defined by location within a protein.

Filtration Methods

Simple methods that can remove gross impurities from protein samples.

Sonication

A method using high frequency sound waves to disrupt cell membranes.

Ion Exchange Chromatography

Method separating proteins based on their net surface charge at a given pH.

Edman Degradation

Method for sequencing amino acids in a polypeptide by tagging the N-terminal residue.

Disulfide Linkages

Stable bonds that hold the polypeptide in a 3D configuration.

Mass Spectrometry (MS)

Technique used to measure mass-to-charge ratios of ionized molecules and determine molecular mass, sequence, and interactions.

Cation Exchange

A technique where negatively charged resin binds positively charged proteins.

Affinity Chromatography

A method that separates proteins based on specific binding interactions between the protein and a ligand.

Size Exclusion Chromatography

Separates molecules based on size by passing them through a column filled with porous beads.