Podcast
Questions and Answers
Which element is uniquely found in proteins compared to carbohydrates and lipids?
Which element is uniquely found in proteins compared to carbohydrates and lipids?
- Hydrogen
- Nitrogen (correct)
- Carbon
- Oxygen
What is the primary role of enzymes within a biological system?
What is the primary role of enzymes within a biological system?
- To catalyze or accelerate chemical reactions (correct)
- To serve as transport molecules for nutrients
- To provide structural support to cells
- To regulate blood sugar levels
Which function is NOT considered a major function of proteins?
Which function is NOT considered a major function of proteins?
- Defense against foreign organisms
- Transport of molecules between cells
- Energy Storage (correct)
- Regulation of bodily functions
How do hormones, which are proteins, primarily contribute to bodily functions?
How do hormones, which are proteins, primarily contribute to bodily functions?
What is the main characteristic that distinguishes fibrous proteins from globular proteins?
What is the main characteristic that distinguishes fibrous proteins from globular proteins?
Which protein type is predominantly found in enzymes and is characterized by its water-soluble nature?
Which protein type is predominantly found in enzymes and is characterized by its water-soluble nature?
What determines the specific properties of each of the 20 different amino acids?
What determines the specific properties of each of the 20 different amino acids?
In the context of amino acids, what chemical behavior does the amino group exhibit?
In the context of amino acids, what chemical behavior does the amino group exhibit?
What type of bond is formed when two amino acids join together?
What type of bond is formed when two amino acids join together?
Given the codon table, if a mutation changes a DNA sequence such that the resulting mRNA codon is UAG, what is the likely effect on protein synthesis?
Given the codon table, if a mutation changes a DNA sequence such that the resulting mRNA codon is UAG, what is the likely effect on protein synthesis?
Which characteristic is associated with the hydrophobic amino acid Valine?
Which characteristic is associated with the hydrophobic amino acid Valine?
Which amino acid is classified as acidic?
Which amino acid is classified as acidic?
Which interaction primarily stabilizes the primary structure of a protein?
Which interaction primarily stabilizes the primary structure of a protein?
Which structural level of a protein is characterized by the arrangement of alpha-helices and beta-sheets?
Which structural level of a protein is characterized by the arrangement of alpha-helices and beta-sheets?
In the context of protein folding, what role do hydrogen bonds play in the formation of alpha-helices and beta-sheets?
In the context of protein folding, what role do hydrogen bonds play in the formation of alpha-helices and beta-sheets?
What type of protein structure results from the combination of alpha helices or beta sheets, or a combination of both?
What type of protein structure results from the combination of alpha helices or beta sheets, or a combination of both?
What is the significance of disulfide bridges in the tertiary structure of a protein?
What is the significance of disulfide bridges in the tertiary structure of a protein?
Which level of protein structure is defined by the interactions between two or more polypeptide chains?
Which level of protein structure is defined by the interactions between two or more polypeptide chains?
Which type of interaction contributes to the quaternary structure of proteins?
Which type of interaction contributes to the quaternary structure of proteins?
How does a slight change in the primary structure of a protein impact its overall function?
How does a slight change in the primary structure of a protein impact its overall function?
Which protein is responsible for transporting oxygen in the bloodstream?
Which protein is responsible for transporting oxygen in the bloodstream?
Which protein provides structural support and is found in skin, tendons, and bones?
Which protein provides structural support and is found in skin, tendons, and bones?
Which protein helps to regulate sugar levels in blood?
Which protein helps to regulate sugar levels in blood?
Which protein is a key component of hair and nails?
Which protein is a key component of hair and nails?
Where is fibroin, a structural protein, commonly found?
Where is fibroin, a structural protein, commonly found?
Which elements are present in ALL proteins?
Which elements are present in ALL proteins?
Where can keratin be found?
Where can keratin be found?
Why are enzymes important in a biological cell?
Why are enzymes important in a biological cell?
Adjacent carboxyl and amino groups...
Adjacent carboxyl and amino groups...
Which protein is involved in muscle contraction?
Which protein is involved in muscle contraction?
Which major function of proteins deals with the protective role against the invasion of foreign organisms?
Which major function of proteins deals with the protective role against the invasion of foreign organisms?
What is the function of thrombin, prothrombin, and fibrinogen?
What is the function of thrombin, prothrombin, and fibrinogen?
Which amino acid is hydrophobic?
Which amino acid is hydrophobic?
Which amino acid is basic?
Which amino acid is basic?
What type of protein is tubulin?
What type of protein is tubulin?
What is an example of a protein that is part of cell membrane?
What is an example of a protein that is part of cell membrane?
What is the function of ribulose biphosphate carboxylase oxydase?
What is the function of ribulose biphosphate carboxylase oxydase?
Where is albumin found??
Where is albumin found??
What is a beta-sheet?
What is a beta-sheet?
What is an alpha-helix?
What is an alpha-helix?
Flashcards
Protein elements
Protein elements
Proteins contain carbon, hydrogen, oxygen, nitrogen, and sulfur.
Proteins structure
Proteins structure
Proteins are key structural components in animals, like horns and feathers.
Proteins building blocks
Proteins building blocks
Proteins are the main building blocks for the body, forming hair, skin, muscles and organs.
Biological catalysts
Biological catalysts
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Proteins transport function
Proteins transport function
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Protein building block
Protein building block
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Enzymes role
Enzymes role
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Hormones function
Hormones function
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Proteins transport
Proteins transport
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Muscle proteins
Muscle proteins
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Structural proteins
Structural proteins
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Proteins defensive
Proteins defensive
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Blood clotting proteins
Blood clotting proteins
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Proteins source of energy
Proteins source of energy
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Cell movement
Cell movement
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Cell membrane proteins roles
Cell membrane proteins roles
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Fibrous protein solubility
Fibrous protein solubility
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Globular protein solubility
Globular protein solubility
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Keratin properties
Keratin properties
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Amino side chain
Amino side chain
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Structure of amino acids
Structure of amino acids
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Dipeptide formation
Dipeptide formation
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Polypeptide formation
Polypeptide formation
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Non polar amino acids name
Non polar amino acids name
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Nonpolar amino acids examples
Nonpolar amino acids examples
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Uncharged polar amino acids
Uncharged polar amino acids
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Charged polar amino acids
Charged polar amino acids
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Protein building blocks
Protein building blocks
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Primary structure
Primary structure
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Secondary structure alpha helix
Secondary structure alpha helix
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Secondary structure beta-sheet
Secondary structure beta-sheet
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Tertiary structure
Tertiary structure
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Quaternary structure
Quaternary structure
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Study Notes
Characteristics of Proteins
- Contain carbon, hydrogen, oxygen, nitrogen, and sulfur.
- Serve as structural components in animals like horns, claws, and feathers.
- Proteins build the body’s materials such as hair, skin, muscles, and organs.
- They catalyze biological reactions as enzymes.
- They act as transport molecules like hemoglobin.
- Amino acids are the basic building block.
Major Functions of Proteins
- Enzymes are biological catalysts involved in digestion, energy capture, and biosynthesis.
- Ribulose biphosphate carboxylase oxydase (photosynthesis), nitrogenase (nitrogen fixation), pepsin (protein digestion) are examples.
- Hormones are involved in the chemical regulation of bodily functions
- insulin and glucagon (blood-sugar level regulation) and growth hormone (stimulates cell growth and division) are exmaples.
- Proteins transport molecules between cells
- hemoglobin, myoglobin, and lipoproteins are examples.
- Serve as contractile elements of muscles
- actin and myosin are examples.
- Offer protection and support as structural components
- collagen, elastin, keratin, and fibroin (silk protein) are examples.
- Provide a protective role against the invasion of foreign organisms by way of defense
- antibodies/immunoglobulins are examples.
- Proteins serve as blood clotting factors to prevent blood loss when blood vessels are damaged
- thrombin, prothrombin, fibrinogen are examples.
- Act as a source of energy
- albumin in eggs and casein in milk are examples.
- Play a role in cellular movement
- cytoskeletal proteins (tubulin & actin) are examples.
- Function as channel or carrier proteins and act as a component of cell membranes.
- integral and peripheral proteins are examples.
Proteins Key Role in Living System
- Catalyze almost all chemical reactions in a living cell by protein enzymes.
- Transport various substances, such as oxygen and ions.
- Transfer information
- hormones are an example
Types of Proteins
- Fibrous proteins are found in the skin, tendons, bones, and muscles
- They are hydrophobic, not dissolving in water.
- Globular proteins exist in enzymes, some hormones, and hemoglobin
- They are hydrophilic, able to dissolve in water.
- Keratin is a family of tough and insoluble fibrous structural proteins
- Forms hard but non-mineralized structures in reptiles, birds, amphibians, and mammals.
- Enzymes accelerate or catalyze chemical reactions
- Almost all processes in a biological cell need enzymes to occur at significant rates.
Amino Acid Structure and Bonds
- Amino acids are the basic unit of any protein.
- Different side chains determine the properties of the 20 amino acids.
- An amino acid consists of an asymmetric carbon covalently bonded to a hydrogen, an amino group, a carboxyl (acid) group, and a variable R group specific to each amino acid.
- The amino group acts like a base and tends to be positive.
- The carboxyl group acts like an acid and tends to be negative.
- "R" groups are variable, from 1 atom to 20.
- Two amino acids form a dipeptide.
- Adjacent carboxyl and amino groups bond together.
- Amino acid + amino acid = dipeptide.
- Amino acid + dipeptide = tripeptide.
- A.A. + A.A. + A.A. + ... = Polypeptide
Characteristics and Properties of Amino Acids
- The three main physical categories:
- Nonpolar "hydrophobic" (9 total): Include Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline, Phenylalanine, and Tryptophan
- Uncharged polar, "hydrophilic" (6 total): Include Serine, Threonine, Asparagine, Glutamine, Tyrosine, and Cysteine
- Charged polar, (5 total), categorized into 2 acidic & 3 basic
- Include Lysine, Arginine, Glutamic acid, Aspartic acid, and Histidine
- R groups (side chains) confer properties, and amino acids are grouped by polarity
- Polar, water soluble
- Non-polar, water insoluble
- Positively charged, or negatively charged (polarity)
Physical Groupings of Amino Acids (with 20 Examples):
- Glycine (G), Alanine (A), Valine (V), Isoleucine (I), Leucine (L), Proline (P), Methionine (M), Phenylalanine (F), Tryptophan (W), Asparagine (N), Glutamine (Q), Serine (S), Threonine (T), Tyrosine (Y), Cysteine (C), Aspartic acid (D), Glutamic acid (E), Lysine (K), Arginine (R), Histidine (H)
- White: Hydrophobic
- Green: Hydrophilic
- Red: Acidic
- Blue: Basic
Structure of a Protein
- Proteins consist of one or more polypeptide chains.
- Four levels of protein structure:
- Primary structure
- Amino acid single covalently-bonded
- Unique sequencing of amino acids
- Genes determine this sequencing
- Alterations in the primary structure change fuction
- Condensation synthesis forms peptide bonds
- Secondary structure
- Repeated folding
- Stabilized by hydrogen bonds between peptide linkages -Alpha helix is a single strand bonded by intramolecular hydrogen bonds -Beta-sheet involves two chains, linked by hydrogen bonds
- Tertiary structure
- Combination of pure helix or pure beta or a combination of both
- Weak chemical bonds -Hydrogen bonds: polar side chains -Ionic bonds: charged side chains -Hydrophobic and van der Waals strong covalent bonds -Disulfide bridges
- Quaternary structure
- Interaction among 2 or more polypeptide chains
- Includes collagen and hemaglobin
- Primary structure
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Description
Learn about the characteristics and major functions of proteins. Proteins contain carbon, hydrogen, oxygen, nitrogen, and sulfur. They catalyze biological reactions as enzymes, act as transport molecules, and serve as structural components in animals.