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What is the significance of amino acid R-groups in proteins?
What is the significance of amino acid R-groups in proteins?
Enzymes and antibodies serve the same primary function in biotechnology.
Enzymes and antibodies serve the same primary function in biotechnology.
False
What technique is used to study proteins through their separation based on size and charge?
What technique is used to study proteins through their separation based on size and charge?
polyacrylamide gel electrophoresis
The enzyme __________ breaks down molecules to regulate nerve impulses between nerve cells.
The enzyme __________ breaks down molecules to regulate nerve impulses between nerve cells.
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Match the following protein functions with their descriptions:
Match the following protein functions with their descriptions:
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Which of the following factors does NOT affect enzyme activity?
Which of the following factors does NOT affect enzyme activity?
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Zinc ions are a cofactor required for the activity of adenosine deaminase.
Zinc ions are a cofactor required for the activity of adenosine deaminase.
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What is the term for the molecule that an enzyme acts on?
What is the term for the molecule that an enzyme acts on?
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The process in which proteins lose their three-dimensional shape is called __________.
The process in which proteins lose their three-dimensional shape is called __________.
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Match the following enzyme models with their descriptions:
Match the following enzyme models with their descriptions:
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What is the optimum pH?
What is the optimum pH?
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Silver stain is less sensitive than Coomassie® Blue for low concentrations of proteins.
Silver stain is less sensitive than Coomassie® Blue for low concentrations of proteins.
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In PAGE, what determines how fast a peptide chain moves through the gel?
In PAGE, what determines how fast a peptide chain moves through the gel?
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What is the first step of protein synthesis?
What is the first step of protein synthesis?
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Translation involves converting mRNA into a sequence of nucleotides.
Translation involves converting mRNA into a sequence of nucleotides.
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What is the role of tRNA in protein synthesis?
What is the role of tRNA in protein synthesis?
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The __________ process splits the polypeptide into two or more strands.
The __________ process splits the polypeptide into two or more strands.
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Match the following terms with their definitions:
Match the following terms with their definitions:
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Which model describes how substrates fit into an enzyme's active site?
Which model describes how substrates fit into an enzyme's active site?
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Enzymes can catalyze all chemical reactions in a cell.
Enzymes can catalyze all chemical reactions in a cell.
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What is the function of the ribosome in protein synthesis?
What is the function of the ribosome in protein synthesis?
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Which level of protein structure is defined by the specific sequence of amino acids?
Which level of protein structure is defined by the specific sequence of amino acids?
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Beta-pleated sheets are a form of primary structure in proteins.
Beta-pleated sheets are a form of primary structure in proteins.
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What is the role of antibodies in the immune response?
What is the role of antibodies in the immune response?
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The technique used to determine the three-dimensional structure of a protein is called ______.
The technique used to determine the three-dimensional structure of a protein is called ______.
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Match the following structures with their definitions:
Match the following structures with their definitions:
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What is the significance of the gp210 structure in HIV?
What is the significance of the gp210 structure in HIV?
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Glycoproteins are proteins that have sugar groups added to them.
Glycoproteins are proteins that have sugar groups added to them.
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The specific region on a molecule that an antibody binds to is known as the ______.
The specific region on a molecule that an antibody binds to is known as the ______.
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Study Notes
Introduction to Studying Proteins
- Proteins are crucial to biotechnology.
- Protein's three-dimensional structure is essential for function.
- Researchers study protein structure and amino acid sequences to create protein products.
Learning Outcomes
- Describe protein structure, emphasizing the role of amino acid R-groups.
- Explain protein synthesis (transcription and translation).
- Discuss the role of naturally occurring and recombinant proteins in biotechnology.
- Classify proteins based on their function (structural, antibody, enzyme).
- Differentiate between antibodies and antigens.
- Distinguish among enzyme classes and reaction conditions impacting enzyme activity.
- Summarize polyacrylamide gel electrophoresis (PAGE) and its use in studying proteins.
5.1 The Structure and Function of Proteins
- Virtually all biotechnology products involve proteins.
- Proteins' three-dimensional structure defines their function.
- To develop a protein product, researchers study protein structure and amino acid sequence.
- X-ray crystallography is a technique that reveals protein structure.
Protein Molecule Structure
- Proteins consist of one or more folded peptide chains made of amino acids.
- Human salivary amylase is an example, with over 500 amino acids.
Amino Acid Structure
- Twenty types of amino acids are found in proteins.
- Most proteins include hundreds of amino acids.
- Amino acids share a common core structure, differing only in their R-group.
Protein 3-D Structure
- Primary structure: the sequence of amino acids in a protein.
- Protein folding is influenced by interactions between amino acids.
- Secondary structure includes alpha helices and beta-pleated sheets.
- Tertiary structure defines the overall 3D protein shape.
- Quaternary structure results from multiple polypeptide interactions.
Impact of Structure on Protein Function
- The precise shape of a protein determines its interaction with other molecules.
- Antibodies recognize and bind foreign molecules for removal.
- Antibodies have a variable region for binding and a constant region for recognition.
5.1 Vocabulary
- X-ray crystallography: technique to determine 3D protein structure.
- Polar: contains both positive and negative charges.
- Primary structure: order and type of amino acids.
- Secondary structure: structure resulting from hydrogen bonds (e.g., alpha helix, beta sheet).
- Tertiary structure: structure formed from interactions involving "R" groups and hydrogen bonds.
- Quaternary structure: structure formed by multiple polypeptide interactions.
- Glycoprotein: protein with added sugar groups.
- Glycosylated: descriptive of a molecule with added sugar groups.
- CD4 cells: human white blood cells with CD4 protein on their surface.
- Antigens: foreign proteins/molecules targeted by antibodies
- Epitope: specific region on a molecule recognized by an antibody.
- ELISA: technique to measure protein/antibody amounts.
- Monoclonal antibody: antibody directed against a single epitope.
- Hybridoma: hybrid cell generating monoclonal antibodies.
5.2 The Production of Proteins
- Proteins were once exclusively produced in cells.
- Small polypeptide chains are now produced in labs using protein synthesizers.
- Protein synthesis is a two-step process: transcription and translation.
- Transcription: Converting DNA code to mRNA.
- Translation: Converting mRNA code into amino acid sequence.
- Protein synthesis occurs constantly within cells.
Transcription and Translation
- DNA's genetic code needs to be converted to mRNA.
- Protein synthesis (transcription and translation) involves crucial steps and molecules.
- The process converts the genetic code (DNA) into a protein.
- mRNA copies the genetic information from DNA.
### Protein Synthesis in Prokaryotes
- Protein synthesis in prokaryotes follows similar principles to that in eukaryotes.
- This process involves a circular single strand of DNA and various molecules like mRNA and tRNA.
5.2 Vocabulary
- Protein synthesis: generation of new proteins from amino acid building blocks.
- Transcription: Process of deciphering DNA code to RNA code.
- Codon: Set of three nucleotides in mRNA coding for a specific amino acid.
- Translation: Process of decoding mRNA into amino acid sequence.
- tRNA: Type of RNA that brings amino acids to the ribosome.
- Peptidyl transferase: Enzyme in ribosomes connecting amino acids.
- Phosphorylation: Addition of phosphate groups to molecules.
- Cleavage: Process of splitting a polypeptide into smaller strands.
- Taq polymerase: DNA synthesis enzyme resistant to high temperatures.
5.3 Enzymes: Protein Catalysts
- Enzymes are proteins acting as catalysts for cellular reactions.
- Enzymes are involved in practically every biochemical reaction.
- Enzymes act on substrates fitting specific active site shapes. This interaction can be described by theories such as lock and key and induced fit model.
- Enzymes' catalytic behaviour depends on different factors.
Enzyme Groups and Functions
- Hydrolases: split substrates using water.
- Lyases: split substrates without water.
- Transferases: move chemical groups between molecules.
- Isomerases: rearrange substrate molecules.
- Oxidoreductases: transfer electrons.
- Synthetases: combine molecules.
- Examples for each enzyme group are provided to illustrate their functions.
Factors That Affect Enzyme Activity
- Substrate concentration: more substrate, faster reaction.
- Temperature: enzymes have optimal temperatures.
- pH: enzymes have optimal pH values.
Optimum pH
- Each enzyme has an optimal pH range for maximum activity.
- pH outside of the optimal range usually reduces enzyme activity.
5.3 Vocabulary
- Substrate: molecule acted upon by an enzyme.
- Cofactors: Atoms/molecules required for enzyme activity.
- Lock and Key Model: Enzyme and substrate fit perfectly.
- Induced Fit Model: Enzyme changes shape to fit substrate.
- Optimum temperature: Temperature for optimal enzyme activity.
- Denaturation: Loss of protein shape (3D structure).
- Optimum pH: pH for maximum enzyme activity.
5.4 Studying Proteins - PAGE
- Protein samples are separated on a polyacrylamide gel using a technique called polyacrylamide gel electrophoresis (PAGE).
- Vertical PAGE gel boxes are similar in operation to horizontal PAGE gel boxes.
- Protein size is determined using protein standards/markers.
- Smaller proteins move faster through the gel.
PAGE – Vertical Gel Electrophoresis
- Vertical PAGE gel boxes have a similar design to horizontal PAGE gel boxes.
- Gel cassettes are snapped or screwed into the box.
- Running buffer covers the wells and the front of the gel cassette.
- Electric current moves negatively charged protein samples down the gel towards the positive electrode.
PAGE with Standards
- The smaller the protein, the faster it migrates through the gel.
- Protein sizing markers/standards allow for the size determination of unknown samples by comparison.
- Protein molecular weight is often represented in kilodaltons (kDa).
Staining Methods
- Silver stain is a much more sensitive staining method to visualize proteins and DNA when concentrations are low.
5.4 Vocabulary
- PAGE: Polyacrylamide gel electrophoresis - Separation of proteins and DNA.
- Coomassie Blue: Dye that stains proteins, making them visible on gel.
- Silver stain: More sensitive stain for protein visualization than Coomassie Blue.
5.5 Applications of Protein Analysis
- Studying protein profiles of cells/tissues provides insights into cellular function.
- Protein structure relates to protein function.
- Understanding proteins provides insights into cellular mechanisms, evolution, and taxonomic relationships.
- The National Center for Biotechnology Information (NCBI) hosts databases and tools for protein and DNA analysis.
5.5 Vocabulary
- Taxonomic relationships: how species are related through evolution.
- Biomanufacturing: industry focusing on protein production through biotechnology.
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Description
This quiz explores the critical role of proteins in biotechnology and their three-dimensional structures essential for function. Participants will learn about protein synthesis, classification, and techniques like polyacrylamide gel electrophoresis. Enhance your understanding of how proteins impact various biotechnological applications.
