Niamh Flashcards
Which of the following best defines proteomics?
A) The study of DNA sequences and their functions
B) The analysis of the entire protein complement in a given cell, tissue, or organism
C) The study of RNA transcription and translation processes
D) The structural characterization of individual amino acids
B
How does the proteome differ from the genome?
A) The proteome is static, while the genome is dynamic
B) The proteome remains unchanged across tissues and conditions
C) The proteome is constantly changing in response to environmental and cellular conditions
D) The proteome consists only of proteins encoded by housekeeping genes
C
Which of the following is a low-throughput method for protein analysis?
A) Mass spectrometry
B) Two-dimensional gel electrophoresis (2D-PAGE)
C) Reverse-phase protein microarrays
B
Which of the following factors contributes to the complexity of the proteome?
A) Alternative splicing
B) Frameshifting
C) Post-translational modifications
D) All of the above
D
Which of the following is NOT a primary function of proteins in a biological system?
A) Catalyzing metabolic reactions
B) Storing genetic information
C) Transmitting cellular signals
D) Regulating gene expression
B
Which of the following best describes post-translational modifications (PTMs)?
A) Changes in gene sequence that affect protein expression
B) Structural modifications to proteins after translation that affect function, localization, or stability
C) DNA modifications that regulate protein expression
D) RNA modifications that enhance protein translation efficiency
B
Which of the following is NOT a challenge in proteomic research?
A) The high dynamic range of protein expression
B) Protein degradation during sample preparation
C) The stability of proteins compared to DNA
D) The complexity of post-translational modifications
C
What is the primary purpose of functional proteomics?
A) To identify the sequence of proteins in an organism
B) To understand the biological roles and interactions of specific proteins
C) To compare protein structures across species
D) To determine the genomic location of protein-coding genes
B
Which proteomic approach is primarily focused on determining which proteins are present in a given tissue or cell type?
A) Protein quantification
B) Protein localization
C) Protein identification
D) Structural proteomics
C
Which of the following best describes top-down proteomics?
A) Proteins are first digested into peptides before analysis
B) Intact proteins are analyzed before fragmentation and further characterization
C) Only small proteins are studied using this method
D) It exclusively uses gel-based separation techniques
B
How does enzyme-linked immunosorbent assay (ELISA) detect specific proteins?
A) By measuring protein degradation over time
B) By using antibodies that bind to target proteins and generate a detectable signal
C) By separating proteins based on molecular weight
D) By directly sequencing proteins using mass spectrometry
B
What is a major limitation of gel-based proteomic methods?
A) Inability to separate proteins by charge
B) Limited sensitivity and difficulty in analyzing low-abundance proteins
C) Inability to detect post-translational modifications
D) Lack of reproducibility across experiments
B
Which of the following is a high-throughput proteomic method?
A) Western blotting
B) Mass spectrometry-based proteomics
C) Gel electrophoresis
D) Affinity chromatography
B
How is proteomics used in drug discovery?
A) It identifies protein targets for drug design and evaluates drug-protein interactions
B) It measures the genetic mutations in a patient’s DNA
C) It replaces traditional pharmacology methods
D) It detects bacterial infections in real time
A
Which of the following describes a major advantage of using proteomics in personalized medicine?
A) It enables tailoring treatments based on an individual’s unique protein expression profile
B) It eliminates the need for genetic testing
C) It replaces all traditional diagnostic methods
D) It focuses solely on metabolic diseases
A
How do mass spectrometry-based methods contribute to proteomics research?
A) By sequencing nucleotides within a genome
B) By identifying and quantifying proteins in a sample based on mass-to-charge ratios
C) By visualizing protein structures through electron microscopy
D) By measuring cellular RNA levels
B
Which of the following is a key application of proteomics in medicine?
A) Identification of protein biomarkers for disease diagnosis
B) Mapping the human genome
C) Predicting nucleotide mutations
D) Analyzing chromosomal abnormalities
A
What is the main advantage of using chromatography-based methods in proteomics?
A) They allow for rapid DNA sequencing
B) They separate proteins based on physical and chemical properties
C) They enable visualization of protein interactions
D) They identify mutations in protein-coding genes
B
Which proteomic technique is most commonly used for analyzing post-translational modifications?
A) Southern blotting
B) Mass spectrometry
C) Polymerase chain reaction (PCR)
D) Fluorescence microscopy
B
Which field of study combines proteomics with systems biology to investigate host-pathogen interactions?
A) Paleoproteomics
B) Structural biology
C) Systems toxicology
D) Functional genomics
C
What is the primary difference between bottom-up and top-down proteomics?
A) Bottom-up proteomics analyzes entire proteins, whereas top-down proteomics studies peptides
B) Bottom-up proteomics involves digesting proteins into peptides before analysis, while top-down proteomics studies intact proteins
C) Top-down proteomics is only used for structural analysis, whereas bottom-up proteomics measures protein abundance
D) Bottom-up proteomics is less commonly used in proteomics research
B
Which of the following is a proteomic application in agriculture?
A) Investigating plant-pathogen interactions and engineering stress-resistant crops
B) Measuring soil pH variations
C) Developing genetically modified animals
D) Monitoring atmospheric nitrogen levels
A
Which gel-based technique separates proteins based on molecular weight using an electric current?
A) 2D-PAGE
B) SDS-PAGE
C) Western blotting
D) ELISA
B
Which of the following best describes the principle behind Western blotting?
A) Proteins are separated by electrophoresis, transferred to a membrane, and detected using enzyme-conjugated antibodies
B) Proteins are digested into peptides before analysis
C) Proteins are labeled with isotopic tags for quantification
D) Proteins are separated based on their binding to a ligand in a column
A
What is the primary function of mass spectrometry in proteomics?
A) Sequencing DNA to determine genetic mutations
B) Measuring the mass-to-charge ratio of peptides and proteins
C) Detecting RNA expression levels in cells
D) Separating proteins based on size and charge
B
Which of the following is NOT a conventional proteomics technique?
A) Enzyme-linked immunosorbent assay (ELISA)
B) Western blotting
C) Chromatography-based separation
D) CRISPR gene editing
D
What is the main advantage of affinity chromatography in protein purification?
A) It separates proteins based on charge variations
B) It isolates proteins based on their specific interactions with ligands
C) It requires no prior knowledge of protein structure
D) It is the fastest method for whole-proteome analysis
B
Which gel-based technique enhances the resolution of protein separation by incorporating fluorescent dyes?
A) Western blotting
B) 2D-DIGE
C) SDS-PAGE
D) Mass spectrometry
B
Which chromatography-based technique separates proteins based on charge?
A) Affinity chromatography
B) Ion exchange chromatography
C) Size exclusion chromatography
D) Gas chromatography
B
Which of the following is a key feature of protein microarrays?
A) They require gel electrophoresis for separation
B) They allow high-throughput protein detection from small samples
C) They analyze DNA sequences instead of proteins
D) They exclusively detect protein mutations
B
What is the major difference between 1D-PAGE and 2D-PAGE?
A) 1D-PAGE separates proteins by mass only, whereas 2D-PAGE separates proteins by isoelectric point and mass
B) 2D-PAGE only works for DNA, while 1D-PAGE works for proteins
C) 1D-PAGE is more sensitive than 2D-PAGE
D) 2D-PAGE does not require any staining techniques
A
Which type of protein microarray is used to study protein–DNA and protein–RNA interactions?
A) Analytical protein microarrays
B) Functional protein microarrays
C) Reverse-phase protein microarrays
D) Western blot-based arrays
B
What is the major limitation of mass spectrometry in proteomics?
A) It cannot be used for protein quantification
B) It requires specialized sample preparation and handling
C) It is unable to analyze post-translational modifications
D) It cannot identify peptides
B
Which of the following is NOT a common ionization method in mass spectrometry-based proteomics?
A) Matrix-assisted laser desorption ionization (MALDI)
B) Surface-enhanced laser desorption/ionization (SELDI)
C) Polymerase chain reaction (PCR)
D) Electrospray ionization (ESI)
C
Which quantitative proteomics technique involves tagging proteins with isobaric tags for relative and absolute quantitation?
A) ICAT
B) iTRAQ
C) SILAC
D) MALDI-TOF
B
What is the primary advantage of iTRAQ over traditional labeling methods?
A) It allows multiplexing, enabling simultaneous quantification of multiple samples
B) It does not require any sample preparation
C) It only works for DNA sequencing
D) It measures protein charge rather than abundance
A
Which technique allows for isotopic labeling of proteins in cell culture for quantitative proteomics?
A) SILAC (Stable Isotopic Labeling with Amino Acids in Cell Culture)
B) ELISA
C) Western blotting
D) Chromatography
A
Which proteomics technique uses chemical labeling reagents for protein quantification?
A) ICAT (Isotope-Coded Affinity Tags)
B) Western blotting
C) Size exclusion chromatography
D) SDS-PAGE
A
Which software platform is widely used for analyzing proteomics data?
A) Perseus
B) BLAST
C) CRISPR-Cas9
D) RT-PCR
A
Which proteomic technology enables the analysis of protein structural changes due to disease?
A) Mass spectrometry
B) SDS-PAGE
C) PCR
D) Fluorescence microscopy
A
What is one limitation of MS-based proteomics?
A) It struggles to quantify low-abundance proteins
B) It cannot identify any proteins
C) It only works for bacterial proteins
D) It is less sensitive than Western blotting
A
Which of the following best describes the role of bioinformatics in proteomics?
A) It sequences proteins using gel electrophoresis
B) It develops algorithms to analyze large and complex proteomics datasets
C) It replaces traditional laboratory techniques with computational models
D) It eliminates the need for mass spectrometry
B
What is the main challenge in proteomics compared to genomics?
A) The dynamic and complex nature of proteins, including post-translational modifications
B) The ease of sequencing proteins
C) The fact that proteins have no functional roles in cells
D) The ability to directly analyze proteins without preparation
A
Which step in mass spectrometry-based proteomics is responsible for separating ions based on their mass-to-charge ratio?
A) Ionization
B) Mass analyzer
C) Protein digestion
D) Data visualization
B
Which of the following is NOT an application of proteomics?
A) Drug discovery
B) Biomarker identification
C) Crop engineering
D) DNA fingerprinting
D
How does bioinformatics contribute to proteomics research?
A) It enables statistical analysis of mass spectrometry data
B) It detects proteins using gel electrophoresis
C) It sequences DNA from protein samples
D) It replaces laboratory experiments
A
