Biology 120 Notes (Part 5) Continuing the Discussion of Macromolecules
Each monosaccharide has a unique form and therefore function.
Glycosidic bonds (linkages) join monosaccharides together through dehydration reactions.
Maltose (grain sugar), lactose (milk sugar), and sucrose (table sugar) are common monosaccharides found in everyday use.
All are created via formation of covalent glycosidic linkages.
Polysaccharides are a long chain of monosaccharides joined by glycosidic linkages.
They may be branched or unbranched and may consist of multiple types of monosaccharides.
Starch is a storage polysaccharide in plants. 1. Plants store sugar as starch. It is composed of glucose monomers in a helix.
Glycogen is a highly branched storage polysaccharide in animals. 2. Animals store sugar as glycogen. It is stored in liver and tissue muscle cells.
Cellulose is a structured polysaccharide in plants. Cellulose is a structural polymer. It makes up most of the plant cell walls.
Chitin is a structural polymer found in cell walls of fungi and exoskeletons of insects and crustaceans.
Peptidoglycan is a structural polysaccharide. 5. Peptidoglycan is a structural polymer found in cell walls.
Macromolecules are large molecules made of small molecules joined together.
(Review: The four classes of organic macromolecules are: proteins, lipids, nucleic acids, and carbohydrates.)
They are a catalyst for enzymes.
Collagen and keratin are part of the structure of proteins.
Proteins transport hemoglobin and membrane proteins.
Proteins defend against antibodies.
Proteins signal hormones.
Proteins assist in movement.
Amino acids are protein monomers.
Most proteins are made from combinations of twenty amino acids.
The twenty amino acids differ only in their unique R-group, or side chain.
Amino acids are linked when a bond forms between a carboxyl group of one amino acid and an amino group of another.
The resulting C-N bond is called a peptide bond.
Polypeptides are a chain of amino acids joined together with peptide bonds.
Proteins are a polypeptide or multiple peptides that have a unique structure and function.
Proteins have unparallel diversity of size, shape, and chemical properties.
Proteins serve diverse functions in cells because structure gives rise to function.
Proteins have four basic structures which are: primary, secondary, tertiary, and quaternary.
The primary structure has a sequence of amino acids.
The secondary structure occurs when polypeptides coil or fold in a certain way.
It can look like an a-helix or B-sheet.
The secondary structure is formed by hydrogen bonds.
Folding results in a final 3-D shape of a polypeptide.
Globular proteins exhibit tertiary structure.
The shape is held together by hydrogen bonds.
Ionic bonds and covalent bonds occur between “R groups.”
Many proteins contain several distinct polypeptide subunits that interact to form a single structure.
The bonding of two or more distinct polypeptide subunits makes up a quaternary structure.
Protein structuring is hierarchal.
Quaternary structure is based on tertiary structure, which is based in part on secondary structure.
All three of the higher-level structures are based on primary structure.
Combined effects of primary, secondary, and tertiary structure, and sometimes quaternary structure allow for diversity in protein form and function.
A denatured (unfolded) protein is unable to function normally.
For example, when an egg is cooked, it cannot go back to being an egg that has not been cracked.
Each monosaccharide has a unique form and therefore function.
Glycosidic bonds (linkages) join monosaccharides together through dehydration reactions.
Maltose (grain sugar), lactose (milk sugar), and sucrose (table sugar) are common monosaccharides found in everyday use.
All are created via formation of covalent glycosidic linkages.
Polysaccharides are a long chain of monosaccharides joined by glycosidic linkages.
They may be branched or unbranched and may consist of multiple types of monosaccharides.
Starch is a storage polysaccharide in plants. 1. Plants store sugar as starch. It is composed of glucose monomers in a helix.
Glycogen is a highly branched storage polysaccharide in animals. 2. Animals store sugar as glycogen. It is stored in liver and tissue muscle cells.
Cellulose is a structured polysaccharide in plants. Cellulose is a structural polymer. It makes up most of the plant cell walls.
Chitin is a structural polymer found in cell walls of fungi and exoskeletons of insects and crustaceans.
Peptidoglycan is a structural polysaccharide. 5. Peptidoglycan is a structural polymer found in cell walls.
Macromolecules are large molecules made of small molecules joined together.
(Review: The four classes of organic macromolecules are: proteins, lipids, nucleic acids, and carbohydrates.)
They are a catalyst for enzymes.
Collagen and keratin are part of the structure of proteins.
Proteins transport hemoglobin and membrane proteins.
Proteins defend against antibodies.
Proteins signal hormones.
Proteins assist in movement.
Amino acids are protein monomers.
Most proteins are made from combinations of twenty amino acids.
The twenty amino acids differ only in their unique R-group, or side chain.
Amino acids are linked when a bond forms between a carboxyl group of one amino acid and an amino group of another.
The resulting C-N bond is called a peptide bond.
Polypeptides are a chain of amino acids joined together with peptide bonds.
Proteins are a polypeptide or multiple peptides that have a unique structure and function.
Proteins have unparallel diversity of size, shape, and chemical properties.
Proteins serve diverse functions in cells because structure gives rise to function.
Proteins have four basic structures which are: primary, secondary, tertiary, and quaternary.
The primary structure has a sequence of amino acids.
The secondary structure occurs when polypeptides coil or fold in a certain way.
It can look like an a-helix or B-sheet.
The secondary structure is formed by hydrogen bonds.
Folding results in a final 3-D shape of a polypeptide.
Globular proteins exhibit tertiary structure.
The shape is held together by hydrogen bonds.
Ionic bonds and covalent bonds occur between “R groups.”
Many proteins contain several distinct polypeptide subunits that interact to form a single structure.
The bonding of two or more distinct polypeptide subunits makes up a quaternary structure.
Protein structuring is hierarchal.
Quaternary structure is based on tertiary structure, which is based in part on secondary structure.
All three of the higher-level structures are based on primary structure.
Combined effects of primary, secondary, and tertiary structure, and sometimes quaternary structure allow for diversity in protein form and function.
A denatured (unfolded) protein is unable to function normally.
For example, when an egg is cooked, it cannot go back to being an egg that has not been cracked.