2.12
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show | Carbon, Hydrogen, Oxygen, and Nitrogen and, Formed from Amino
Acids
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show | all proteins contain carbon, hydrogen, oxygen, and nitrogen and are the most abundant
organic molecules in the body
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show | monomer for proteins
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show | Support
Movement
Transport
Buffering
Metabolic regulation
Coordination and control
Defense
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show | organic polymers that consist of long chains if similar organic molecules
called amino acids
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show | amino acids in the body
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show | covalent bond between carboxyl group of one amino acid and the amino group of
another.
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Peptides | show 🗑
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Dipeptide | show 🗑
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show | molecule created containing 3 or more amino acids
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show | proteins; familiar
proteins include hemoglobin, collagen, and keratin.
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show | sequence of amino acids along the length of single polypeptide.
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Secondary structure: | show 🗑
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Tertiary structure: | show 🗑
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Quaternary structure: | show 🗑
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Globular proteins | show 🗑
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Globular proteins.. | show 🗑
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Fibrous proteins | show 🗑
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Fibrous proteins... | show 🗑
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Shape of a protein determines its ... | show 🗑
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show | local environmental conditions
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show | Reactants in enzymatic reactions
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show | Special region of enzyme that substrates must bind to
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show | Substrate binds to active site of enzyme.
Once bound to the active sites, the substrates are held together, making their interaction easier. Substrates binding alters the shape of the enzyme, and this change promotes product
formation.
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show | Product detaches from enzyme; entire process can now be repeated
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show | Each enzyme catalyzes only one type of reaction.
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Saturated | show 🗑
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Saturation Limit | show 🗑
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show | An ion or a molecule that must bind to an enzyme before substrates can also bind.
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Without a cofactor, | show 🗑
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With a cofactor, | show 🗑
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Coenzyme | show 🗑
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Temperature and PH... | show 🗑
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Denaturation | show 🗑
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Denaturation example | show 🗑
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show | combination of protein and carbohydrate molecules
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show | Large proteins with small carbohydrate groups attached
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show | Large polysaccharide molecules linked by polypeptide chains
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