Characteristics and Functions of Proteins
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Questions and Answers

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?

  • 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?

  • 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?

<p>By regulating chemical processes (A)</p> Signup and view all the answers

What is the main characteristic that distinguishes fibrous proteins from globular proteins?

<p>Fibrous proteins are structural and insoluble, while globular proteins are functional and soluble. (D)</p> Signup and view all the answers

Which protein type is predominantly found in enzymes and is characterized by its water-soluble nature?

<p>Globular protein (A)</p> Signup and view all the answers

What determines the specific properties of each of the 20 different amino acids?

<p>The variable R group (C)</p> Signup and view all the answers

In the context of amino acids, what chemical behavior does the amino group exhibit?

<p>It acts like a base, tending to be positive (B)</p> Signup and view all the answers

What type of bond is formed when two amino acids join together?

<p>Peptide bond (D)</p> Signup and view all the answers

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?

<p>Termination of protein synthesis, as UAG is a stop codon (B)</p> Signup and view all the answers

Which characteristic is associated with the hydrophobic amino acid Valine?

<p>It is nonpolar and water-insoluble (D)</p> Signup and view all the answers

Which amino acid is classified as acidic?

<p>Glutamic acid (D)</p> Signup and view all the answers

Which interaction primarily stabilizes the primary structure of a protein?

<p>Peptide bonds (D)</p> Signup and view all the answers

Which structural level of a protein is characterized by the arrangement of alpha-helices and beta-sheets?

<p>Secondary structure (D)</p> Signup and view all the answers

In the context of protein folding, what role do hydrogen bonds play in the formation of alpha-helices and beta-sheets?

<p>They stabilize the structure by forming between peptide linkages. (C)</p> Signup and view all the answers

What type of protein structure results from the combination of alpha helices or beta sheets, or a combination of both?

<p>Tertiary structure (C)</p> Signup and view all the answers

What is the significance of disulfide bridges in the tertiary structure of a protein?

<p>They provide strong covalent linkages for stability (A)</p> Signup and view all the answers

Which level of protein structure is defined by the interactions between two or more polypeptide chains?

<p>Quaternary structure (D)</p> Signup and view all the answers

Which type of interaction contributes to the quaternary structure of proteins?

<p>Hydrophobic interactions (A)</p> Signup and view all the answers

How does a slight change in the primary structure of a protein impact its overall function?

<p>It can alter the protein's function (C)</p> Signup and view all the answers

Which protein is responsible for transporting oxygen in the bloodstream?

<p>Hemoglobin (B)</p> Signup and view all the answers

Which protein provides structural support and is found in skin, tendons, and bones?

<p>Collagen (A)</p> Signup and view all the answers

Which protein helps to regulate sugar levels in blood?

<p>Insulin (B)</p> Signup and view all the answers

Which protein is a key component of hair and nails?

<p>Keratin (B)</p> Signup and view all the answers

Where is fibroin, a structural protein, commonly found?

<p>Silk (B)</p> Signup and view all the answers

Which elements are present in ALL proteins?

<p>Carbon, hydrogen, oxygen, and nitrogen (B)</p> Signup and view all the answers

Where can keratin be found?

<p>Hair (D)</p> Signup and view all the answers

Why are enzymes important in a biological cell?

<p>They speed up processes in the cell. (C)</p> Signup and view all the answers

Adjacent carboxyl and amino groups...

<p>Bond together. (C)</p> Signup and view all the answers

Which protein is involved in muscle contraction?

<p>Actin (B)</p> Signup and view all the answers

Which major function of proteins deals with the protective role against the invasion of foreign organisms?

<p>Defense (A)</p> Signup and view all the answers

What is the function of thrombin, prothrombin, and fibrinogen?

<p>Prevent blood loss when blood vessles are damaged (A)</p> Signup and view all the answers

Which amino acid is hydrophobic?

<p>Isoleucine (D)</p> Signup and view all the answers

Which amino acid is basic?

<p>Lysine (A)</p> Signup and view all the answers

What type of protein is tubulin?

<p>Cellular movement (B)</p> Signup and view all the answers

What is an example of a protein that is part of cell membrane?

<p>Integral and peripheral proteins (C)</p> Signup and view all the answers

What is the function of ribulose biphosphate carboxylase oxydase?

<p>Photosynthesis (B)</p> Signup and view all the answers

Where is albumin found??

<p>Eggs and milk (D)</p> Signup and view all the answers

What is a beta-sheet?

<p>Two chains that are linked by hydrogen bonds (B)</p> Signup and view all the answers

What is an alpha-helix?

<p>One strand of amino acid chain, bonded by hydrogen bonds (B)</p> Signup and view all the answers

Flashcards

Protein elements

Proteins contain carbon, hydrogen, oxygen, nitrogen, and sulfur.

Proteins structure

Proteins are key structural components in animals, like horns and feathers.

Proteins building blocks

Proteins are the main building blocks for the body, forming hair, skin, muscles and organs.

Biological catalysts

Proteins act as biological catalysts, known as enzymes.

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Proteins transport function

Proteins transport molecules like hemoglobin carries oxygen.

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Protein building block

The basic building block of a protein is the amino acid.

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Enzymes role

Enzymes are biological catalysts that facilitate processes like digestion and energy capture.

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Hormones function

Hormones regulate bodily functions, like insulin controlling blood sugar.

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Proteins transport

Proteins transport molecules between cells, such as hemoglobin.

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Muscle proteins

Proteins form contractile elements in muscles, like actin and myosin.

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Structural proteins

Some proteins provide protection and support, like collagen forming silk

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Proteins defensive

Proteins have a protective role against foreign organisms; antibodies provide defense.

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Blood clotting proteins

Proteins include blood clotting factors that prevent blood loss when vessels are damaged.

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Proteins source of energy

Proteins can serve as a source of energy; albumin in eggs is an example.

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Cell movement

Proteins facilitate cellular movement through cytoskeletal proteins.

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Cell membrane proteins roles

Proteins act as channels or carriers in the cell membrane.

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Fibrous protein solubility

Fibrous proteins are found in skin and tendons and are insoluble in water.

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Globular protein solubility

Globular proteins include enzymes and some hormones and are water-soluble.

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Keratin properties

Keratin is a family of tough and insoluble fibrous structural proteins.

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Amino side chain

Different side chains distinguish the 20 amino acids.

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Structure of amino acids

Amino acids consist of an asymmetric carbon bonded to hydrogen, amino group, carboxyl group and variable R group.

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Dipeptide formation

Amino acids join together to form a dipeptide.

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Polypeptide formation

Amino acid connected to amino acid makes dipeptide and then tripeptide, then polypeptide.

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Non polar amino acids name

The term hydrophobic nine (9)

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Nonpolar amino acids examples

They are glycine, alanine, valine, leucine, isoleucine, methionine, proline, phenylalanine and tryptophan

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Uncharged polar amino acids

Serine, threonine, asparagine, glutamine tyrosine, cysteine

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Charged polar amino acids

Lysine, arginine, glutamic acid, aspartic acid, and histidine

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Protein building blocks

A protein consists of one or more polypeptide

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Primary structure

Composed of single covalently-bonded amino acids

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Secondary structure alpha helix

One strand of amino acid chains that is bonded by intramolecular hydrogen bonds

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Secondary structure beta-sheet

Two chains that are link by hydrogen bonds

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Tertiary structure

Combination of pure helix or pure beta or a combination of both

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Quaternary structure

Results from the interactions among 2 or more polypeptide chains

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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

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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.

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