proteins. proteins proteins do the nitty-gritty jobs of every living cell. proteins are made of long...
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PROTEINS
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Proteins• Proteins do the nitty-gritty jobs of every
living cell.
• Proteins are made of long strings of individual building blocks known as amino acids.
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Amino acids contain an amino group, a carboxyl group, a carbon
and a unique R group
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3.2.2
• Identify amino acids ... from diagrams showing their structure.
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Polar R groups make the amino acid hydrophilic
Non-polar R groups make the amino acid hydrophobic
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Ionic R groups make the amino acid hydrophilic
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7.5.3
• Explain the significance of polar and non-polar amino acids.
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There are 20 commonly occurring amino acids that are found in proteins
• alanine - ala - A • arginine - arg - R ***• asparagine - asn - N • aspartic acid - asp - D • cysteine - cys - C • glutamine - gln - Q • glutamic acid - glu - E • glycine - gly - G • histidine - his - H ***• isoleucine - ile - I
• leucine - leu - L • lysine - lys - K • methionine - met - M • phenylalanine - phe - F • proline - pro - P • serine - ser - S • threonine - thr - T • tryptophan - trp - W • tyrosine - tyr - Y • valine - val - V
“Essential Amino Acids” are those that must be ingested in the diet
(our body can’t make them)
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Peptide Bonds join amino acids
It’s a condensation reaction(meaning that H20 is releasedwhen the bond is formed).
Two amino acids form a DI-PEPTIDE
POLYPEPTIDESare formed from more than two amino acids bonded together
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• 3.2.5 Outline the role of condensation and hydrolysis in the relationships between … amino acids and polypeptides.
• 7.4.5 Draw and label a diagram showing the structure of a peptide bond between two amino acids.
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Proteins have four levels of organization
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Primary structure is the amino acid sequence
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The amino acid sequence is coded for by DNA and is unique for
each kind of protein
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The amino acid sequence determines how the polypeptide will fold into its 3D shape
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Even a slight change in the amino acid sequence can
cause the protein to malfunction
For example,
mis-formed hemoglobin causes sickle cell disease
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Proteins have four levels of organization
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Secondary structure results from hydrogen bonding between the oxygen of one amino
acid and the hydrogen of another
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The alpha helix is a coiled secondary structure due to a hydrogen bond every
fourth amino acid
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The beta pleated sheet is formed by hydrogen bonds between parallel
parts of the protein
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A single polypeptide may have portions with both types of
secondary structure
Link to video
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Proteins have four levels of organization
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Tertiary structure depends on the interactions among the R group side chains
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Types of interactions
• Hydrophobic interactions: amino acids with nonpolar side chains cluster in the core of the protein, out of contact with water
= charged
= hydrophobic
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Types of interactions
• Hydrogen bonds between polar side chains
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Types of interactions
• Ionic bonds between positively and negatively charged side chains
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Types of interactions• Disulfide bridge (strong covalent bonds)
between sulfur atoms in the amino acid cysteine
Link to video
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Proteins have four levels of organization
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Quaternary structure results from interactions among separate
polypeptide chains.
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For example, hemoglobin is composed of
4 polypeptide chains
Link to video
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Proteins have four levels of organization
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The folding of proteins is aided by other proteins, called chaperones
• Act as temporary braces as proteins fold into their final conformation
• Research into chaperones is a area of research in biology
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7.5.1
• Explain the four levels of protein structure, indicating the significance of each level.
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Denaturation results in disruption of the secondary, tertiary, or
quaternary structure of the protein
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Denaturation may be due to changes in pH, temperature or
various chemicals
–
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Protein function is lost during denaturation, which is often irreversible
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3.6.4
• Define denaturation.
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Folded proteins are placed into two general categories
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Fibrous proteins have polypeptide chains organized in long fibers or sheets
• Water insoluble
• Very tough physically, may be stretchy
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Functions of fibrous proteins
• Structural proteins function in support– Insects and spiders
use silk fibers to make cocoons and webs
– Collagen and elastin are used in animal tendons and ligaments
– Keratin is the protein in hairs, horns and feathers
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Functions of fibrous proteins• Contractile
proteins function in movement
– Actin and myosin contract to create the cleavage furrow and to move muscles
– Contractile proteins move cilia and flagella
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Globular proteins have their chains folded into compact, rounded shapes
• Easily water soluble
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Functions of globular proteins
• Storage proteins function in the storage of amino acids– Ovalbumin is the protein in
egg whites
– Casein is the protein in milk, source of amino acids for baby mammals
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Functions of globular proteins• Transport proteins function in the movement of
other substances
– Hemoglobin, the iron containing protein in blood, transport oxygen from lungs to other parts of the body (C3032H4816O872N780S9Fe4)
– Membrane transport proteins such as channels for potassium and water
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Functions of globular proteins
• Hormone proteins function as cellular messenger molecules that help maintain homeostasis
– Insulin: sends message “allow sugar into cells” (when blood glucose levels are high, cells will transport glucose into the cells for use or storage)
– Glucagon: sends message “we need more sugar in the blood” (when blood glucose is too low, cells will release glucose)
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Functions of globular proteins
• Receptor proteins allow cells to respond to chemical stimuli
– Growth factor receptors initiate the signal transduction pathway when a growth hormone attaches
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Functions of globular proteins– Cholesterol receptors on the cell
membrane allow LDL to be endocytosed into the cell
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Functions of globular proteins
• Protective proteins function as protection against disease– Antibodies combat bacteria and viruses
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Functions of globular proteins• Enzymes speed up chemical reactions
– Amylase and other digestive enzymes hydrolyze polymers in food
– Catalase converts hydrogen peroxide H2O2 into water and oxygen gas during cellular respiration
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7.5.2
– Outline the difference between fibrous and globular proteins, with reference to two examples of each protein type.
7.5.4
– State four functions of proteins, giving a named example of each.