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    Chapter 6 Chemistry of Proteins (Compatibility Mode)

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    This chapter discusses protein chemistry and classification. It defines proteins as polymers of amino acids coded by genes that serve important roles in cells. It classifies proteins into different types and describes the chemical structure of amino acids. The chapter also details the classification of amino acids, essential amino acids, properties of amino acids, digestion and absorption of proteins, protein requirements, and excess protein consumption risks.

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    Chapter 6 Chemistry of Proteins (Compatibility Mode)

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    This chapter discusses protein chemistry and classification. It defines proteins as polymers of amino acids coded by genes that serve important roles in cells. It classifies proteins into different types and describes the chemical structure of amino acids. The chapter also details the classification of amino acids, essential amino acids, properties of amino acids, digestion and absorption of proteins, protein requirements, and excess protein consumption risks.

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    This chapter discusses protein chemistry and classification. It defines proteins as polymers of amino acids coded by genes that serve important roles in cells. It classifies proteins into different types and describes the chemical structure of amino acids. The chapter also details the classification of amino acids, essential amino acids, properties of amino acids, digestion and absorption of proteins, protein requirements, and excess protein consumption risks.

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    © All Rights Reserved
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    17 views28 pages

    Chapter 6 Chemistry of Proteins (Compatibility Mode)

    Uploaded by

    bayan.gr
    This chapter discusses protein chemistry and classification. It defines proteins as polymers of amino acids coded by genes that serve important roles in cells. It classifies proteins into different types and describes the chemical structure of amino acids. The chapter also details the classification of amino acids, essential amino acids, properties of amino acids, digestion and absorption of proteins, protein requirements, and excess protein consumption risks.

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    GENERAL

    BIOCHEMISTRY
    BIOC 201

    CHAPTER VI
    Chemistry of Proteins
    Objectives
     One objective of this chapter is
    getting the student to understand
    proteins chemistry and types.
     The chapter will detail the basic
    classification of amino acids.
     To provide the student with hints
    about the metabolic pathways of
    proteins.
    PROTEINS are:
    polymers of amino acids
    coded from genes
    the work horses of biological systems
    the key roles in constructing and
    maintaining living cells
    Protein types:
    Enzymes
    Hormones
    Storage proteins
    Transport proteins
    Structural proteins
    Protective proteins (antibodies)
    Toxic proteins
    Protein Chemistry
    Proteins are organic compounds contain
    alpha amino acids united by peptide
    linkages.
    They are composed of C, H, O and N2.
    Amino Acids:
    Contain amino group (NH2) and
    carboxylic group (COOH)
    Chemical Classification of amino acids

    Amino Acids

    Aliphatic aa Aromatic aa Heterocyclic aa

    Neutral aa
    Mono amino-mono carboxylic acid

    Acidic aa
    Mono amino-dicarboxylic acid

    Basic aa
    Diamino-monocarboxylic acid
    Aliphatic amino acids
    Contain NO ring structure

    Glycine: α-amino acetic acid

    Alanine: α-amino propionic acid

    Serine: β-hydroxy α-amino propionic acid

    Threonine

    Valine
    Leucine

    Isoleucine

    Cysteine

    Cystine (Two molecules of cysteine united by S-S bond)

    Methionine

    Homoserine
    Acidic amino acids

    Aspartic acid

    Glutamic acid
    Basic amino acids

    Arginine

    Ornithine

    Lysine

    Hydroxylysine
    Aromatic amino acids
    Having aromatic ring

    Phenylalanine

    Tyrosine: p-hydroxy-phenylalanine
    Heterocyclic amino acids
    Having Heterocyclic ring

    Tryptophane: α-amino- β-indole propioinc


    acid

    Hisitidine: α-amino- imidazole propioinc


    acid
    Heterocyclic amino acids (cont.,)
    Having Heterocyclic ring

    Proline

    Hydroxyproline

    HO---
    Amino Acids (aa):
     9 of the 20 amino acids must be completely obtained
    from the diet and ONE* must be partially obtained
    from diet
     These are referred to as the essential amino acids
    (TPLVI HAMLT)
     Threonine Histidine
     Phenylalanine Arginine*
     Leucine Methionine
     Valine Lysine
     Isoleucine Tryptophan
     Proteins are also the major source of nitrogen in the diet
    Nutritional Classification
    Nutritional Classification
    N.B.: Arginine and Histidine are essential for
    growing animals but not for adults.
    Semiessential aa

    Proteins containing all essential a.a. are


    called proteins of high biological value.
    Metabolic Classification
    1. Glucogenic amino acids:
    give Glucose
    Glycine, serine, arginine and glutamic acid
    2. Ketogenic amino acids:
    give ketone bodies (Leucine)
    3. Glucogenic and Ketogenic amino
    acids: give both…
    Phenylalanine, tyrosine, tryptophan, isoleucine and lysine.
    Amino Acids Properties
    All are α-amino acids
    Majority are L-amino acids
    All are optically active
    (except glycine)
    Glycine doesn’t contain asymmetric carbon atom
    Amino Acids Properties
    Amphoteric properties:
    In acidic medium, they act as base
    carrying (+) charges.
    In alkaline medium, they act as acids
    carrying (-) charges.
    In certain pH, they carry both (+) and (-),
    i.e. electrically neutral.
    This is called isoelectric point
    (IEP)
    Amino Acids Properties
    Isoelectric point (IEP):
    It is the pH at which the amino acid or
    protein carries both (+) and (-) charges and
    so its electrically neutral.
    It is called (ZWITTER ION) or (dipolar
    ion).
    Amino acid mixture can be separated and identified by a
    technique called Thin Layer Chromatography (TLC)
    Digestion

    No digestion in the mouth


    it begins in the stomach
    Hydrochloric acid denatures protein and
    also converts pepsinogen to pepsin
    Pepsin breaks the proteins into small
    peptides of various lengths and a. a.
    Pepsin completes ~ 10-20% of digestion
    Digestion (cont.,)

    Pancreas makes trypsinogen and


    chymotrypsinogen (proenzymes)
    They will be activated to trypsin and
    chymotrypsin (proteases)
    Proteases break down polypeptides into
    smaller peptides (very few peptides have
    been broken down to amino acids at this
    stage)
    Absorption:
    most protein absorbed in the duodenum
    and jejunum
    >99% of protein enters the blood stream
    as amino acids
    whole protein absorption can cause a
    severe allergic reaction
    How Much Protein Do We Need?
    Adults:
    0.8 grams per kilogram of body weight per
    day (0.8/kg/day)

    Endurance Athletes:
    1.2 to 1.4 g/kg/day

    Heavy Weight Trainers:


    1.7 to 1.8 g/kg/day
    Protein quality
    Complete Proteins:
    provide all the essential amino acids
    (animal proteins)
    High biological value
    Incomplete Proteins:
    are missing one or more essential amino
    acids (Low biological value)
    (plant proteins except soy protein)
    Incomplete proteins can be served with a
    complementary protein to make it complete
    Excess dietary protein

    May strain the kidneys


    May cause mineral losses
    (especially calcium)*
    May increase risk of obesity*
    May increase risk of heart disease*
    May increase risk of cancer*
    *only with animal protein

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