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Biomolecules
The organic molecules that are essential to living organisms
The 4 primary classes of biomolecules
1) Carbohydrates
2) Proteins
3) Nucleic Acids
4) Lipids
Monomers
Single, individual building blocks that can be repetitively linked together to form polymers
Monomers vary?
Depending on the type of biomolecule polymer
Consistent and not consistent monomers
Carbohydrates, Proteins and nucleic acids use consistent monomers to form polymers, but lipids do NOT
Dehydration Synthesis
Forms covalent bonds to link individual monomers and build a polymer
Hydrolisis
Breaks covalent bond to break down a polymer
Carbohydrates
Carbon-based-molecules hydrated with many hydroxyl groups (-OH)
What is carbohydrates referred to
Saccharides
Simple Carbohydrates
Fit Cn(H2O)n formula exactly
Complex Carbohydrates
Can differ slightly from Cn(H2O)n and can have P,N or S atoms
Monosaccharide
A single carbohydrate unit or monomers
Oligosaccharide
2 to 20 covalently linked monosaccharides
Polysaccharides
More than 20 covalently linked monosaccharides (polymer)
Glycosidic Bonds
Covalent bonds that link monosaccharides together
Hydrolysis
Breaks down polysaccharides into individual monosaccharides
What are the two main functions of a carbohydrate
Storage Support: Helps build
Energy Storage: Used for short-term energy-storage
Cellulose
Most abundant carbohydrate found in plant-cells
Starch
Storage form of glucose in plants
Chitlin
Found in the exoskeleton of a insect or crustaceans
Glycogen
Storage form of glucose in animals
Proteins
A class of biomolecule polymers made of amino acid monomers
Peptide Bonds
Covalent bonds linking adjacent amino acids together
Proteins polymers have directionality
N-terminal and C-terminal Ends
Amino Acids
The monomers of proteins
Amino Acids: Nonpolar Side Chains; Hydrophobic
Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, Proline (9)
Amino Acids: Electrically charge side chains; hydrophilic
Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine (6)
Amino Acids: (Negatively Charged)
Aspartic Acid, Glutamic acid
Amino Acids: (positively charged)
Lysine, Arginine, Histidine
1st protein related term
Amino Acids: A single protein unit or monomer
2nd protein-related terms
Oligo peptide: 2 to 20 covalently linked amino acids
3rd Protein related terms
Peptide: Less than 50 covalently linked amino acids
4th Protein-related terms
Polypeptide: Greater than 50 covalently linked amino acids
5th Protein-related terms
Protein: One or multiple polypeptide chains in their folded/functional forms
Primary Protein Structure
Types, quantity, and order of amino acids. Determines all other levels of structure
Secondary Protein structure
Formation of either alpha-helics or Beta-sheets in the protein backbone
Tertiary protein structure
Overall 3D-shape of a polypeptide chain
Quaternary Protein structure
Multiple polypeptide chains associate to form a single, functional protein
Why is a proteins structure and shape critical
Its critical for its proper function
Denatured Protein
A non-functional protein that has altered its shape
What causes a denatured protein
pH, Temp, or salt concentration
Chaperone Proteins
Chaperone Proteins
Proteins that help other proteins can re-form their shape (or renature)
Nucleic acids
A class of biomolecule polymers that store/ encode genetic information
Directionality of the nucleic acid polymer
5’ and 3’ ends
Nucleotide monomers consist of 3 components
1) Phosphate Group
2) Pentose Sugar
3) Nitrogenous base
Nitrogenous Basses: Pyrimidines
Single-ringed molecules
Cytosine, Thymine, Uracil
Nitrogenous Bases: Purines
Double Ringed Molecules
Adenine, Guanine
Nitrogenous bases on different DNA strands pair together
A with T and C with G
Phosphodiester Bonds
The covalent bonds that link nucleotides together
Results in the sugar-phosphate “Backbone”
Directionality of 5’ phosphate end to 3’ hydroxyl end
Deoxyribonucleic acid (DNA)
Stores genetic/hereditary information in the cell.
Forms a double-helix 2 anit-parallel strands connected by base-pair hydrogen bonds
Ribonucleic acid (RNA)
Has a variety of functions including acting as a template for synthesizing proteins
Usually forms a single-stranded nucleotide chain
Lipids
Hydrophobic biomolecules insoluble in water that are highly diverse in their structure and function
Can be amphipathic: Having both hydrophobic and hydrophilic group
Do not form polymers
Lipids include
Fats, oils, phospholipids, steroids, and waxes
Fats and oils
Long term energy storage in animals and plants
Phospholipids
Major component of cell membranes
Steroids
Component of plasma membrane and hormones
Waxes
Protection and prevention of water loss
Fatty acids
Hydrocarbon chains of varying length with a carboxylic acid
Saturated Fatty acids
Fully saturated with hydrogens (only contains C-C single bonds)
Solids at room temp
Unsaturated Fatty acids
Not fully saturated with hydrogens due to presence of more than 1 C=C double bond
-Double bond creates a bend in the chain making them liquids at room temp
Trans-fat
Artificial unsaturated fatty acids that are NOT bent (linear)
Triglycerides
A lipid with 3 fatty acid chains covalently linked to a single glycerol molecule
Fatty acids linked to glycerol results in
Dehydration synthesis reactions
Phospholipids
Large class of lipids that contain a phosphate group
Major component of all cell membranes
Amphipathic molecules with a hydrophilic head and hydrophobic tails
Steroids
Lipids that are made of 4 fused carbon ring structures
Cholesterol
Common steroid important for the structure of animal cell membranes
Waxes
Another class of lipid that can be used for protection and prevention of water loss