proteins have many functions, some examples of these functions are?
- enzymatic proteins: act to speed up chemical reactions.
- storage proteins: store amino acids.
- hormonal proteins: help to maintain homeostasis.
- contractile and motor proteins: involved in movement.
- defensive proteins: help to protect us from disease.
- transport proteins: transport substances.
- structural proteins: provide a role in support.
- receptor proteins: mediate the response of a cell to a chemical stimulus.
give an example for each of the proteins!
- enzymatic protein: salivary amylase.
- storage protein: ovalbumin
- hormonal protein: insulin
- contractile and motor protein: actin and myosin
- defensive protein: antibodies
- transport protein: hemoglobin
- structural protein: collagen
- receptor protein: receptor on nerve cells
proteins are made up of monomers called?
amino acids.
how many amino acids are used to make proteins?
20 amino acids are used to build proteins in living organisms.
what are amino acids?
organic molecules possessing both carboxyl and amino groups, they differ in their properties due to differing side chains called r groups.
the structure of an amino acids?
amino group, carboxyl group, hydrogen atom, and r group.
different types of amino acids and examples for each?
- nonpolar side chains: hydrophobic: alanine
- polar side chains: hydrophilic: serine
- electrically charged: acidic or basic
acidic: side chain negative charge due to ionized carboxyl group: aspartic
basic: side chain positive charge: lysine
how are the amino acids joined together to form a polymer?
dehydration reaction.
the bond that is formed between two amino acids is called?
a peptide bond.
how does a peptide bond form?
a peptide bond forms when a carboxyl group from one amino acid reacts with the amino acid of a second amino acid. resulting in a polypeptide.
polypeptide vs protein?
a polypeptide is a chain of amino acids linked together by peptide bonds. a protein is a functional molecule made up of one or more polypeptide chains that have folded into a specific, three-dimensional structure. proteins have complex secondary, tertiary, and sometimes quaternary structures
some facts about proteins?
- protein has biological activity
- proteins are stable
- conformation is unique for each protein
- depends on the sequence of amino acids in the polypeptide and how the side groups of each amino acid interact with one another.
what does a proteins specific conformation determine?
determines how it functions.
a protein can be broken down into how many levels of organization?
primary structure, secondary structure, tertiary structure, and quaternary structure.
what is primary structure?
the primary structure of a protein refers to its linear sequence of amino acids linked together by peptide bonds.
what is secondary structure?
folding or coiling of the polypeptide resulting in a a helix or b pleated sheet.
- results from the hydrogen bonding between the molecules of the backbone.
- r groups are not involved.
what is tertiary structure?
overall 3 dimensional shape of a polypeptide.
- results from interactions between the r groups of amino acids.
TYPES OF BONDS?
what is quaternary structure?
overall protein structure that results from the aggregation of two or more polypeptide subunits.
- ex: collagen, hemoglobin
- not all proteins have this structure
TYPES OF BONDS?
two main classes of protein structure?
fibrous and globular.
fibrous proteins?
structural, support, strength
globular proteins?
enzymes, hormones, transport
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The Chemical Context of Life34
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Chemical Bonds19
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Water12
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Carbon17
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Carbohydrates26
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Lipids19
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Nucleic Acids23
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DNA Replication25
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Proteins21
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Enzymes36
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Tour of the Cell37
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Organelles2
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Membrane Structure & Function55
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Cell Cycle52
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Meiosis I41
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Meiosis II15
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History of Life on Earth6
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Mendel and the Gene Idea48
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Variation in Mendelian Genetics28
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Sex Linkages19
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Protein Synthesis39
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Translation26
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Mutations33
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photosynthesis11
