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    3 Proteins

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    Team BEE
    This document discusses proteins, including their structure and functions. It describes how proteins are composed of amino acid chains and how their structures form at multiple levels - primary, secondary, tertiary, and sometimes quaternary. The document also categorizes protein functions and explains how environmental changes can cause proteins to denature and lose their normal shape.

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    © All Rights Reserved
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    3 Proteins

    Uploaded by

    Team BEE
    73 views42 pages
    This document discusses proteins, including their structure and functions. It describes how proteins are composed of amino acid chains and how their structures form at multiple levels - primary, secondary, tertiary, and sometimes quaternary. The document also categorizes protein functions and explains how environmental changes can cause proteins to denature and lose their normal shape.

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    3 PROTEINS

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    This document discusses proteins, including their structure and functions. It describes how proteins are composed of amino acid chains and how their structures form at multiple levels - primary, secondary, tertiary, and sometimes quaternary. The document also categorizes protein functions and explains how environmental changes can cause proteins to denature and lose their normal shape.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    73 views42 pages

    3 Proteins

    Uploaded by

    Team BEE
    This document discusses proteins, including their structure and functions. It describes how proteins are composed of amino acid chains and how their structures form at multiple levels - primary, secondary, tertiary, and sometimes quaternary. The document also categorizes protein functions and explains how environmental changes can cause proteins to denature and lose their normal shape.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    of 42

    Lesson 5.

    Proteins

    General Biology 11/2


    Science, Technology, Engineering, and Mathematics
    Having a source of
    protein in our diet is
    very important.
    Proteins help us grow
    faster and stronger.
    2
    Athletes utilize proteins
    more frequently
    because their muscles
    are prone to tear
    during their training
    regimen.
    3
    How would you describe the
    structure and functions of
    proteins?

    4
    Learning Competencies
    At the end of the lesson, you should be able to do the following:

    ● Categorize the biological molecules (proteins)


    according to their structure and function
    (STEM_BIO11/12-Ii-j-15).

    5
    Learning Objectives
    At the end of the lesson, you should be able to do the following:

    ● Describe the structure and functions of proteins.

    ● Describe the different classes of proteins.

    6
    Protein Structure

    Amino acid structure


    ● Amino acids have:
    ○ Central carbon
    ○ Amino group
    ○ Carboxyl group
    ○ Hydrogen atom
    ○ R group
    The basic structure of an amino acid.

    7
    Protein Structure

    The twenty amino acids in living organisms have different R groups


    (highlighted in blue), which give them varying chemical properties in
    the cell's physiological conditions. 8
    Protein Structure

    The twenty amino acids in living organisms have different R groups


    (highlighted in blue), which give them varying chemical properties in
    the cell's physiological conditions. 9
    Protein Structure

    The twenty amino acids in living organisms have different R groups


    (highlighted in blue), which give them varying chemical properties in
    the cell's physiological conditions. 10
    Protein Structure
    The Classification of Amino Acids Based on their Chemical Nature

    Hydrophobic Hydrophilic

    Nonpolar Polar Acidic Basic

    Glycine Phenylalanine Serine


    Alanine Tryptophan Cysteine
    Aspartic acid Lysine
    Valine Methionine Tyrosine
    Glutamic acid Arginine
    Leucine Proline Threonine
    Histidine
    Isoleucine Asparagine
    Glutamine
    11
    Protein Structure

    Peptide Bond Formation


    ● Cells link amino acid
    monomers together by
    dehydration reactions.

    ● The bond between


    adjacent amino acids is
    In the process of a dehydration
    called a peptide bond. reaction, one amino acid releases an
    H+, and the other releases OH–. Thus,
    a water molecule is produced. 12
    Levels of Protein Structure

    Primary Secondary

    Levels of Protein Structure

    Tertiary Quaternary
    13
    Levels of Protein Structure

    The primary protein structure refers to the unique sequence


    of amino acids. 14
    Levels of Protein Structure

    Secondary protein structures include the alpha-helices and beta-sheets,


    which resulted from amino acid chain coiling or folding. 15
    Levels of Protein Structure

    Tertiary structures of proteins are formed and maintained by


    hydrophobic, hydrophilic, and ionic interactions, as well as by disulfide
    bridges. 16
    Levels of Protein Structure

    Hemoglobin is an example of a protein that can attain a quaternary


    structure. It has four polypeptides, wherein each has primary, secondary
    and tertiary structures. 17
    Protein Structure

    Protein Denaturation
    ● Some conditions can
    cause a protein to
    unravel and lose its
    normal shape.
    ○ Examples of these
    conditions include
    The change in the appearance and
    pH and temperature. chemical composition of an egg once
    cooked is primarily because of protein
    denaturation.
    18
    Why can denatured proteins no
    longer perform their normal
    functions?

    19
    Functional Classification of Proteins

    Structural Storage Enzymes

    Functional Classifications
    of Proteins

    Transport Messengers Contractile

    20
    Functional Classification of Proteins

    Structural Proteins

    The keratin in hair and silk in spider webs are examples of structural
    proteins. Keratin can also be found in the horns, claws, hooves, and outer
    skin of vertebrates.
    21
    Functional Classification of Proteins

    Enzymes

    Enzymes are mostly globular proteins that catalyze reactions. They are very
    specific to the substrate molecule or reactants, the reactions of which are
    catalyzed.
    22
    Functional Classification of Proteins

    Transport Proteins

    Channel and carrier proteins allow the movement of different molecules


    across the cell membrane.
    23
    Functional Classification of Proteins

    Immune Proteins

    Interactions between antigens and antibodies help trigger immune


    responses. 24
    Functional Classification of Proteins

    Chemical Messengers

    Insulin consists of two amino acid chains connected by disulfide bridges (in
    yellow color) between cysteine residues. 25
    Functional Classification of Proteins

    Contractile Proteins

    Contractile proteins are present in muscle cells, which helps the body to
    initiate various forms of movements. 26
    Functional Classification of Proteins

    Storage Proteins

    Storage proteins provide amino acids for growing organisms, such as


    germinating seeds and developing embryos in eggs.
    27
    How are proteins involved in
    the different metabolic
    processes?

    28
    Check Your Understanding

    Write true if the statement is correct and false if it is


    otherwise.
    1.The twenty 20 amino acids can be grouped according to
    whether their R group is hydrophobic or hydrophilic.
    2.Tertiary protein structure consists of more than one
    polypeptide.
    3.An unfavorable change in the condition of the
    environment cannot affect the shape of proteins.

    29
    Check Your Understanding

    Briefly explain the possible consequences should the


    following events take place.
    1.All amino acids have the same side groups.
    2.Some gene mutations resulted in an impaired urea
    cycle.
    3.The body does not produce ammonium ions.

    30
    Let’s Sum It Up!

    ● Proteins are biological compounds composed of


    chains of amino acid monomers. Proteins, given
    the variety of their structures, have diverse
    functions in living organisms.

    31
    Let’s Sum It Up!

    ● Each amino acid consists of a central carbon that


    is bonded to four covalent groups. Three of these
    four attachments are common to all 20 amino
    acids—an amino group (—NH2), a carboxyl
    group (—COOH), and a hydrogen atom. The
    variable component of amino acids, the R group
    (radical group), is attached via the fourth bond of
    the central carbon.
    32
    Let’s Sum It Up!

    ● A peptide consists of two or more amino acids


    bonded together, and the resulting longer chain of
    amino acids joined by peptide bonds is called a
    polypeptide. A protein is a polymer consisting of
    one or more polypeptides.

    33
    Let’s Sum It Up!

    ● The overall shape of a protein has at least three


    levels of structure, which are primary, secondary,
    and tertiary structures. Proteins with more than
    one polypeptide chain have a fourth level called the
    quaternary structure.

    34
    Let’s Sum It Up!

    ● Protein shape is sensitive to the surrounding


    environment. Any unfavorable change in
    temperature, pH, salt, or some other cellular
    conditions may result in denaturation or loss of
    normal protein function.

    35
    Let’s Sum It Up!

    ● Proteins are, in many ways, important to living


    organisms. Proteins may function to provide
    structure, storage, catalysis, transport,
    chemical signaling, motility, and immunity.

    36
    Let’s Sum It Up!

    ● Protein digestion involves various enzymes


    produced by the stomach, pancreas, and small
    intestine. After absorption, amino acids are
    transported to the liver and other body tissues for
    further metabolism.

    37
    Let’s Sum It Up!

    ● One byproduct of amino acid metabolism is


    ammonium. The urea cycle in the liver allows the
    processing of ammonium ions so that they can be
    excreted in the urine.

    38
    Let’s Sum It Up!

    Graphical representation of structure, functions, and metabolic


    activities involving proteins 39
    Photo Credit

    ● Slide 19: This photo, Protein Denaturation by RMADLA, is licensed under CC-BY SA 3.0 via
    Wikimedia Commons.

    40
    Bibliography

    Hoefnagels, Marielle. Biology: The Essentials. 2nd ed. McGraw-Hill Education. 2016.

    Mader, Sylvia S., and Michael Windelspecht. Biology. 11th ed. McGraw-Hill Education. 2014.

    “Protein Metabolism.” BC Campus. Accessed April 17, 2020.


    https://opentextbc.ca/anatomyandphysiology/chapter/24-4-protein-metabolism/.

    Reece, Jane B, Martha R. Taylor, Eric J. Simon, Jean L. Dickey, and Kelly Hogan. Biology Concepts and
    Connections. 8th ed. Pearson Education South Asia, Pte Ltd., 2016.

    Simon, Eric J., and Jane B. Reece. Campbell Essential Biology. 5th ed. Pearson Education Inc., 2013.

    41
    Bibliography

    Starr, Cecie, Christine A. Evers, and Lisa Starr. Biology Applications and Concepts. 8th ed. Cengage
    Learning Asia Pte. Ltd., 2012.

    Starr, Cecie, Christine A. Evers, and Lisa Starr. Biology: Today and Tomorrow. 4th ed. Cengage Learning
    Asia Pte. Ltd., 2014.

    42

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