Proteomics and Mass Spectrometry – Core Vocabulary

Vocabulary flashcards covering key terms and methods from lectures on proteomics and mass spectrometry.

Proteome

The complete set of proteins expressed by a cell, tissue, or organism at a specific time under defined conditions.

Proteomics

The large-scale study and characterization of the proteome, including protein expression levels, structures, functions, and interactions.

Mass Spectrometry (MS) in Proteomics

An analytical technique that ionizes peptides/proteins, measures their mass-to-charge ratios, and enables protein identification and quantification.

2D-GE (Two-Dimensional Gel Electrophoresis)

A protein-separation method that first resolves proteins by isoelectric point and then by molecular weight on orthogonal gel axes.

2D-DIGE (Two-Dimensional Difference Gel Electrophoresis)

An advanced 2D-GE technique that labels different protein samples with distinct fluorescent dyes, allowing simultaneous separation and quantitative comparison on the same gel.

Typical MS Proteomics Workflow

A sequence of steps: protein extraction → enzymatic digestion to peptides → separation (e.g., LC) → ionization (ESI/MALDI) → mass analysis → data processing and database search.

Quantitative Proteomic Approaches

Methods for measuring relative or absolute protein abundance, including label-free quantification, stable isotope labeling (e.g., SILAC), and isobaric tagging (iTRAQ, TMT).

Biomedical Applications of Proteomics

Use of proteomic data to identify disease biomarkers, study pathophysiology, discover drug targets, and monitor treatment responses.

Protein Quantification

The process of determining the amount of each protein present in a sample, often achieved through MS-based intensity measurements or isotope-labeled standards.

Proteomic Experimental Strategies

Integrated approaches (2D-GE, 2D-DIGE, MS-based workflows) designed to separate, identify, and quantify proteins in complex biological samples.