UNIT 1: Macromolecules Flashcards
Macromolecules
- Often polymers
- Long molecules built by linking together small similar sub units
- All polymers (macromolecules) are built by dehydration synthesis
Polymers
Substance consisting of very large molecules
- Bonds within polymers are strong covalent bonds so needs a high temperature to break
Carbohydrates
- Simple sugars called monosaccharides
- Shortest chain are 3 Carbons
- Can be distinguished by placement of carbonyl group and # of Carbons
- Fast source of energy
- Broken down into glucose
Monosaccharides
- Simple sugars (fructose, glucose & galactose)
- Contains 3-7 Carbons
- Combine through glycosidic bonds to form larger carbohydrates
- Produce and store energy
- Often form rings
Disaccharides
- Carbohydrate polymer composed of two monosaccharides (sucrose, lactose, maltose)
- Joined by glycosidic bonds
- Act as an energy source
- Our body breaks them down into monosaccharides for digestion
Polysaccharide
- molecules made up of monosaccharide sub units
- Polymers which contains hundreds of sugar molecules bonded together (starch, cellulose, glycogen)
- Store energy in organisms
- Beta glycosidic bonds
Lipids
- Include fatty acids, fats & Oils, sterols and phospholipids
- Two building blocks, fatty acid and glycerol
- Great source for long term energy
- Make up lipid bi-layer
- Help move and store energy
- Synthesized in smooth ER
Glycerol
- Triol compound
- Backbone is found in lipids known as glycerides
- Main function is energy storage
- Lipid esters of the glycerol molecule and fatty acids
Saturated fatty acids
- in animals
- All internal Carbon bonded to at least two H atoms
- Single covalent bonds
- High melting point
Proteins
- Long chains of amino acids
- Act as enzymes, build muscle and work in immune system
- Performs many cellular functions
Enzymes
Made of proteins that act as a catalyst
Cytokines
- Category of a small protein
- peptides that cannot cross the lipid bi-layer into the cytoplasm
Anti-bodies
- Y shaped blood protein that counteracts a specific antigen
Amino Acid
- Molecules that combine to form proteins
- When proteins are broken down, amino acids are left
- Break down food, grow and repair body tissue
Peptide bond
Link two amino acids to form short or long chains
Polypeptide
- Composed of amino acids linked by covalent bonds called peptide bonds
- Short chain (amino acid) or long chain (protein)
- When polypeptides are linked together they are called sub units
- When they get tertiary structure they become functional proteins
Glycine
Amino acid that has a single H atom as its side chain
Denaturation
- Process in which proteins or nucleic acids lose their secondary, tertiary and quaternary structure
- Is reversible meaning primary structure must be alive (not destroyed)
Nucleic Acid
- Composed of nucleotides
- Made up of a pentose sugar, nitrogenous base and a phosphate group
- Nitrogenous bases have weak hydrogen bonds
- Purines and pyrimidines
- DNA encodes info used to assemble proteins
- RNA reads DNA encoded info to direct protein synthesis
Bipolymers
Natural polymers produced by the living cells of organisms
Nucleotides
Form the basic structural unit of nucleic acid; such as DNA
Ribose sugar
Simple, single ring pentose sugar
Organelle
An organelle is a sub-unit within a cell that has a specialized function
Osmosis
Movement of water molecules from solution with high [ ] of water to one with low [ ] of water through cells partially permeable membrane
Unsaturated fatty acid
- at least one double bond between Carbon atoms
- A double bond forms a kink in the structure
- Low melting point
Polyunsaturated fatty acid
- More than one double bond between Carbons
- Usually in plants
- liquid at room temperature
Fats and oils
- Built by dehydration synthesis
- Consists of glycerol molecule with three attached fatty acids (triglyceride/triglycerol)
Monomers
Building blocks for many molecules
What is an aldehyde?
Carbonyl group located at the top of a chain
(example: glucose)
What is an ketone?
Carbonyl group located in the middle of a chain (example: fructose)
Pyrimidines
- Consists of cytosine, thymine and uracil
- One nitrogenous ring
- Forms Hydrogen bonds
- Smaller than purines
Purines
- Consists of adenine and guanine
- Two nitrogenous rings
- Forms Hydrogen bonds
- Larger in size
DNA
- Deoxyribonucleic acid composed of nucleotides to form nucleic acids
- Contains deoxyribose sugar
- Double stranded and forms a helix
- Has H attatched to its second Hydrogen
RNA
- Ribonucleic acid composed of nucleic acids to form nucleotide
- Contains ribose sugar
- Single stranded and does not form helix
- Less stable than DNA
- Acts as an enzyme
- First hereditary material
- Store genetic info as DNA
- Transcribes parts into mRNA which then directs protein synthesis
- Suggests genes came before enzymes
Nucleic acids
- Polymerize by adding to the 3’ hydroxyl group (Phosphodiester bonds form)
- Raw polymerizing units are nucleotide triphosphate
- Strands run from 5’ to 3’
- 5’ Carbon has its own phosphate group
- Strands are anti-parallel and are complimentary to each other
Phosphodiester bonds
Formed between pentose sugars by strong covalent bonds (linked between nucleotides)
Phospholipids
- Hydrophilic head and hydrophobic tails
- Contains saturated and unsaturated fatty acids (depending on kinks)
- Glycerol (polar)
- Phosphate groups (non-polar)
- Amphipatic
- Self assemble
Primary structure
- Linear sequence of amino acids
- Bonded by peptide bonds
Secondary structure
- Alpha helical structure
- Beta pleated sheet structure
- Stabilized by Hydrogen bonds
Tertiary structure
- 3D shape of a single polypeptide molecule
- Uses a variety of different bonds including;
Hydrogen bonds
Hydrophobic interactions
Ionic bonds
Covalent bonds (disulfide bridges) between cysteine amino acids
Quaternary structure
- Assembly of several polypeptides
- Uses same bond types tertiary structure uses
Chaperones
Special proteins that help new proteins fold correctly
Common functional groups
- Hydroxyl group
- Amino group
- Carbonyl group
- Carboxyl group
- Phosphorous group
- sulfihydryl group
All hydrophilic
Amino basic structure
What is the ratio?
1:2:1
Beta gylycosidic bonds
- OH is above the plane
- includes plants, chitin, cellulose and insects
Alpha glycosidic bonds
- OH on Carbon 1’ is below glucose ring
- Includes polysaccharides; starch, glycogen, cellulose
Isotopes
Atoms of an element that posses a different number of neutrons
Radioactive isotopes
- Spontaneously decay into elements of lower atomic numbers
- Emits energy and or subatomic particles
Electronegativity
- Electrons are drawn towards nucleus
- Atom is more electronegative when there are more protons in the nucleus
- Farther out electrons are, the weaker they feel the positive charge
- Oxygen is most electronegative in bio
What is a compound?
Composed of two or more different types of atoms in a particular ratio
Protenoids
Chains of amino acids that form without mRNA information (abiotically, no genes)
Protopoints
- Don’t reproduce precisely
- Show some characteristics of life
- Maintain homeostasis
- May show properties like metabolism and excitability
Cell theory
- Cells are the smallest unit with properties of life
- All organisms are composed of one or more cells
- Cells are created from the growth and division of pre-existing cells
Origins of life
- Prokaryotes were the first cells, then branched into archae and bacteria (3.5-2 BYA)
- 2.5 BYA oxygen started appearing from photosynthesis
- 2.7 BYA oxygen started accumulating in atmosphere
- Hot sand, clay and rocks have been shown to facilitate polymerization
Seven characteristics of life
- A displayed order
- Harness and utilize energy
- Reproduce
- Responds to stimuli
- Exhibit homeostasis
- Ability to evolve
- Growth and development
Abiotic synthesis
Describes the synthesis of organic compounds from inorganic precursors
Sterols
- Type of lipid
- Steroid nucleus: 4 fused rings (almost planar)
- Various non-polar alkyl side chains
- All eukaryotic cells contain different sterols
- Maintains constant membrane fluididity
- Hormones are cholesterol derivitaves
Amino group
- Different amino acids include;
non-polar amino acids
uncharged amino acids
charged amino acids - NH2
Carbonyl group
- Aldehydes which has C double bond O connected to a Hydrogen atom
- Ketones which has C double bond O connected to other Carbon atoms
Carboxyl group
- Organic acid
- COOH or C double bond O, single bond OH
Hydroxyl group
- Alcohol group
- OH
Phosphate group
- Nucleic acids, nucleotides etc
- PO3 2-
Sulfihydryl group
- Many cell molecules
- SH
Amphiatic properties
When a molecule has both hydrophilic and hydrophobic properties
Hydrocarbons
- Consists of Carbons and Hydrogens
- non-polar covalent bonds form
- Modifies properties in functional groups
- Not very soluble in water
- Loosely held (low electronegativity)
