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    Biochem Check For Understanding

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    Maria Vannesa Anne Salvacion
    Proteins are composed of amino acid chains and play crucial roles in the structure, function, and regulation of cells. They have diverse functions including serving as enzymes, providing structure, transporting molecules, regulating processes, immune defense, storage, muscle movement, and cell signaling. The primary elements in proteins are carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur. There are nine essential amino acids that humans must obtain through diet as we cannot synthesize them, and 11 non-essential amino acids that the body can synthesize. Protein folding involves four levels - primary, secondary, tertiary, and quaternary structure - to achieve the functional shape. Diseases like marasmus and kwashiorkor result from severe protein deficiency

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    Biochem Check For Understanding

    Uploaded by

    Maria Vannesa Anne Salvacion
    31 views5 pages
    Proteins are composed of amino acid chains and play crucial roles in the structure, function, and regulation of cells. They have diverse functions including serving as enzymes, providing structure, transporting molecules, regulating processes, immune defense, storage, muscle movement, and cell signaling. The primary elements in proteins are carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur. There are nine essential amino acids that humans must obtain through diet as we cannot synthesize them, and 11 non-essential amino acids that the body can synthesize. Protein folding involves four levels - primary, secondary, tertiary, and quaternary structure - to achieve the functional shape. Diseases like marasmus and kwashiorkor result from severe protein deficiency

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    BIOCHEM

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    BIOCHEM CHECK FOR UNDERSTANDING

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    Proteins are composed of amino acid chains and play crucial roles in the structure, function, and regulation of cells. They have diverse functions including serving as enzymes, providing structure, transporting molecules, regulating processes, immune defense, storage, muscle movement, and cell signaling. The primary elements in proteins are carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur. There are nine essential amino acids that humans must obtain through diet as we cannot synthesize them, and 11 non-essential amino acids that the body can synthesize. Protein folding involves four levels - primary, secondary, tertiary, and quaternary structure - to achieve the functional shape. Diseases like marasmus and kwashiorkor result from severe protein deficiency

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    31 views5 pages

    Biochem Check For Understanding

    Uploaded by

    Maria Vannesa Anne Salvacion
    Proteins are composed of amino acid chains and play crucial roles in the structure, function, and regulation of cells. They have diverse functions including serving as enzymes, providing structure, transporting molecules, regulating processes, immune defense, storage, muscle movement, and cell signaling. The primary elements in proteins are carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur. There are nine essential amino acids that humans must obtain through diet as we cannot synthesize them, and 11 non-essential amino acids that the body can synthesize. Protein folding involves four levels - primary, secondary, tertiary, and quaternary structure - to achieve the functional shape. Diseases like marasmus and kwashiorkor result from severe protein deficiency

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    of 5

    CHECK FOR UNDERSTANDING

    1. Define proteins.
    ANSWER: Proteins are large, complex molecules that play a crucial role in
    the structure, function, and regulation of almost every aspect of cells and
    organisms. They are one of the four major macromolecules essential for life,
    alongside carbohydrates, lipids, and nucleic acids (DNA and RNA). Proteins
    are composed of chains of smaller building blocks called amino acids, which
    are linked together in a specific sequence.

    2. What are the functions of proteins?


    ANSWER:

    The functions of proteins are incredibly diverse and include:

    Enzymatic Functions: Many proteins act as enzymes, which are biological


    catalysts that facilitate and accelerate chemical reactions in cells. Enzymes
    are essential for processes such as digestion, metabolism, and DNA
    replication.

    Structural Functions: Some proteins provide structural support to cells and


    tissues. For example, collagen is a protein that forms the structural framework
    of skin, tendons, and bones.

    Transport Functions: Proteins are involved in the transport of molecules within


    cells and throughout the body. Hemoglobin, for instance, transports oxygen in
    the bloodstream.

    Regulatory Functions: Proteins play a key role in regulating various cellular


    processes. Hormones are a type of regulatory protein that control activities
    like growth, metabolism, and the immune response.

    Defense Functions: Antibodies are proteins that are part of the immune
    system and help the body defend against pathogens such as bacteria and
    viruses.

    Storage Functions: Some proteins serve as reservoirs for essential molecules.


    For instance, ferritin stores iron in the body.

    Contractile Functions: Muscle contractions are made possible by proteins like


    myosin and actin, which are responsible for the movement of muscles.

    Signaling Functions: Signaling proteins transmit information within and


    between cells, allowing for communication and coordination of cellular
    activities.

    3. What are the elements present in proteins?


    ANSWER: Proteins are composed of a specific combination of elements,
    primarily carbon (C), hydrogen (H), oxygen (O), nitrogen (N), and sometimes
    sulfur (S). These elements combine in various ways to form the building
    blocks of proteins, which are amino acids. Here's a breakdown of the key
    elements present in proteins:

    Carbon (C): Carbon is a fundamental element in all organic compounds,


    including proteins. It forms the backbone of amino acids, creating a chain-like
    structure.

    Hydrogen (H): Hydrogen atoms are attached to carbon and nitrogen atoms in
    the amino acid backbone. They also play a role in the interactions that help
    stabilize the three-dimensional structure of proteins.

    Oxygen (O): Oxygen atoms are present in various functional groups within
    amino acids, such as carboxyl (-COOH) and hydroxyl (-OH) groups. These
    functional groups participate in chemical reactions within proteins.

    Nitrogen (N): Nitrogen is a crucial element in proteins because it makes up a


    significant portion of the amino groups (-NH2) found in amino acids. Nitrogen
    atoms in amino acids are involved in forming peptide bonds that link individual
    amino acids together to create a protein chain.

    Sulfur (S): Sulfur is not present in all amino acids, but it is a component of two
    amino acids: cysteine and methionine. Sulfur atoms in cysteine can form
    disulfide bonds (S-S bonds) with other cysteine residues in the same or
    different protein chains, which can greatly influence protein structure and
    stability.

    In summary, carbon, hydrogen, oxygen, nitrogen, and, in some cases, sulfur


    are the primary elements present in proteins. The unique arrangement of
    these elements within the amino acid sequence determines the three-
    dimensional structure and function of a protein.

    4. Identify the essential and non-essential amino acids.


    ANSWER:

    Essential Amino Acids: Essential amino acids are amino acids that the
    human body cannot synthesize in sufficient quantities or cannot synthesize at
    all. Therefore, they must be obtained through dietary sources. There are nine
    essential amino acids for humans:

    a. Phenylalanine
    b. Valine
    c. Threonine
    d. Tryptophan
    e. Methionine
    f. Leucine
    g. Isoleucine
    h. Lysine
    i. Histidine

    These amino acids are crucial for protein synthesis and various physiological
    functions. A balanced diet that includes a variety of protein sources typically
    provides these essential amino acids.

    Non-Essential Amino Acids: Non-essential amino acids are amino acids


    that the human body can synthesize on its own, so they do not need to be
    obtained from the diet. There are 11 non-essential amino acids for humans:

    a. Alanine
    b. Arginine
    c. Asparagine
    d. Aspartic acid
    e. Cysteine
    f. Glutamine
    g. Glutamic acid
    h. Glycine
    i. Proline
    j. Serine
    k. Tyrosine

    The body can produce these amino acids from various metabolic pathways,
    using precursor molecules and enzymes. While they are termed "non-
    essential," they are still essential for overall protein synthesis and other
    biochemical processes.

    5. What is protein folding and briefly explain the four levels of protein folding
    mechanism.
    ANSWER: Protein folding is the process by which a protein structure
    assumes its functional shape. There are four stages of protein folding:
     Primary structure: the sequence of amino acids held together by peptide
    bonds.
     Secondary structure: the protein beginning to fold up, generated by
    formation of hydrogen bonds between atoms in the polypeptide backbone,
    which folds the chains into either alpha helices or beta-sheets.
     Tertiary structure: formed by the folding of the secondary structure sheets
    or helices into one another.
     Quaternary structure: the final shape of the protein, formed by the
    combination of two or more polypeptide chains.

    6. What is marasmus? Explain briefly the relationship of protein to this


    disease.
    ANSWER: Marasmus is a severe form of protein-energy malnutrition. It is
    caused by a person's inability to ingest adequate protein and calories, which
    leads to depletion of proteins and breakdown of other tissues. Energy levels
    plummet and key processes cease, leading to dangerous low energy levels
    and vital functions stopping. Marasmus affects both adults and children, but it
    most often affects young children in developing countries. Protein is essential
    to prevent Marasmus. The body uses proteins for fuel, so their depletion leads
    to breakdown of other tissues because they aren't being replaced. Without
    adequate protein intake, the body cannot function properly and Marasmus can
    occur.

    7. What is kwashiorko? Explain briefly the relationship of protein to this


    disease.
    ANSWER: Kwashiorkor is a severe form of malnutrition associated with a low
    protein diet. It mainly occurs in children and is more common in areas affected
    by famine, economically backward communities, and lack of education can
    also contribute to this condition. People with kwashiorkor are especially
    deficient in protein, as well as some key micronutrients. Severe protein
    deficiency causes fluid retention in the tissues (edema), which distinguishes
    kwashiorkor from other forms of malnutrition. Protein is essential for the
    growth and repair of tissues in the body. Inadequate consumption of protein is
    the main reason for kwashiorkor. Kwashiorkor occurs in people who may have
    access to carbohydrates but lack protein in their diet.

    8. What is meant by isoelectric point? What is its importance?

    ANSWER: The isoelectric point (pI), also known as the isoionic point, is a
    specific pH value at which a molecule, such as a protein or an amino acid,
    carries no net electrical charge. At the isoelectric point, the molecule is
    electrically neutral because the number of positively charged groups (protons,
    H⁺ ions) is equal to the number of negatively charged groups (hydroxide ions,
    OH⁻) within the molecule. In other words, it is the pH at which the molecule's
    acidic and basic functional groups are fully ionized, resulting in a net charge of
    zero.

    The importance of the isoelectric point lies in several key areas:

    Protein Chemistry: In the context of proteins, the isoelectric point is a crucial


    parameter that helps determine their solubility and behavior in different pH
    environments. Proteins are amphoteric molecules, meaning they can act as
    both acids (donating protons) and bases (accepting protons). The pI of a
    protein influences its net charge, which, in turn, affects its interactions with
    other molecules, its folding, and its stability.

    Electrophoresis: Isoelectric focusing is a technique in electrophoresis that


    separates molecules like proteins based on their pI. By applying an electric
    field in a pH gradient, molecules will migrate toward their isoelectric point,
    where they become immobilized due to their net charge being zero. This
    technique is valuable for separating and characterizing proteins in research
    and clinical applications.
    Peptide and Amino Acid Chemistry: Amino acids and peptides also have
    isoelectric points. Understanding the pI of these molecules is important in
    analytical chemistry and biochemistry for techniques such as peptide
    purification and chromatography.

    Biological Function: The isoelectric point of proteins can have implications for
    their biological function. For example, enzymes often have optimal activity at a
    specific pH close to their pI. Changes in pH away from the pI can affect the
    charge distribution on the enzyme's active site and, consequently, its activity.

    Drug Development: In the pharmaceutical industry, the isoelectric point of a


    drug molecule can influence its solubility, stability, and absorption in the body.
    Knowledge of the pI is important when formulating drugs to ensure they are
    effective and have suitable pharmacokinetic properties.

    In summary, the isoelectric point is a critical concept in biochemistry and


    related fields because it helps us understand and manipulate the behavior of
    molecules like proteins and amino acids in various biochemical and analytical
    contexts. It is a fundamental parameter for characterizing and studying the
    properties of biomolecules.

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