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Acidic pH level and chemical balance
- pH < 7
- Hydroxide < Hydrogen
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Which molecule is the primary energy source for cells?
ATP
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Polymers and 2 examples
- Multiple monomers that come together to form large chemical compounds.
- Ex. Carbs and Proteins
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Catabolic
- Large chemicals broken into smaller ones
- Cata - to break
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The two types of metabolic reactions
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Which molecule is a combination of a carbohydrate and 2 inorganic molecules?
Glucose (C₆H₁₂O₆)
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Types of carbohydrates and their descriptions
- Monosaccharides - 1 sugar unit
- Disaccharides - 2 sugar units
- Polysaccharides - many sugar units (form rings)
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Examples of monosaccharides
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Monomer
A single molecule that can react with other monomers
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Disaccharide makeup and creation process
Two monosaccharides put together by dehydration synthesis
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What are isomers? Give an example.
- Isomers are chemicals that have the same chemical formula but a different arrangement of molecules
- Glucose and fructose
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Metabolism
All the chemical reactions in cells
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Basic (alkaline) pH level and chemical balance
- pH > 7
- Hydroxide > Hydrogen
-
Neutral pH and chemical balance
- pH ~ 7
- Hydroxide = Hydrogen ions
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Polysaccharide definition and different storage types for plants and animals
- Many monosaccharides put together
- Plant storage: Starch
- Plant structure: Cellulose
- Animal storage: Glycogen
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What is the difference between glycogen, starch, and cellulose?
The extent of cross branching causing different properties
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Functions of lipids
- Structural materials - cell membranes, cushion for delicate organs, carriers for fat soluble vitamins
- Energy reservoirs - excess glycogen in animals is converted into fat
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The 4 lipid groups
- Triglycerides (fats/oils)
- Phospholipids (membranes)
- Waxes
- Sterols (cholesterol/steroids)
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Triglycerides
Union of 3 fatty acids with glycerol
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Animal triglycerides
- Fats
- Saturated (stable)
- Single bonds (covalent)
- Difficult for our bodies to digest
-
Plant triglycerides
- Oils
- Poly unsaturated
- Some double bonds
- Easier for our bodies to break down
-
Phospholipids
- 2 fatty acids and a phosphate group
- Fat tail (hydrophobic)
- Phosphate heads hydrophilic - good for cell membranes as its semi-permeable
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Steroids lipid group and hormone group
- Sterols
- Androgen - male sex hormones
- Estrogen - female sex hormones
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Liposome
- Double layered sphere used to:
- - Carry drugs through the body that would otherwise be
- rejected
- - Gene-therapy to introduce new DNA to cells
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Problem with lipids
Fats contain double the amount of energy as an equivalent mass of carbohydrates of proteins
-
LDL (low-density lipoprotein)
Bad cholesterol that clogs arteries
-
HDL (high-density lipoprotein)
Good cholesterol that carries LDLs to the liver to be broken down
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Formation of proteins
- Polypeptides
- Formed from 8 - 1000 amino acids joined to the acid group by peptide (covalent) bonds by dehydration synthesis
-
What all is composed of proteins?
- Ribosomes
- Mitochondria
- Muscles, nerves, skin, hair (mostly protein)
- Antibodies and enzymes (specialized proteins)
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Dehydration synthesis
Forms peptide (covalent) bonds; makes proteins
-
Hydrolysis reaction
Splits protein to make amino acids
-
The body can not produce these (obtained in diets)
Essential amino acids
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Primary Structure
Linear (order of amino acids)
-
What is molecular biology and give example
- Each type of protein has a unique primary structure chain of amino acids
- Ex. Iysozyme
-
Secondary protein structure and what it's caused by
- Coiled or folded
- Difference because of hydrogen bonds
-
What is the coiled protein shape called?
Alpha Helix
-
What is the folded protein shape called?
Beta-pleated sheet
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Tertiary protein
Irregular contortions from R group bonding
-
Quaternary protein
2 or more polypeptide structures aggregated into 1 macromolecule
-
What three things can change a protein's shape/function?
- 1) Excess heat
- 2) Radiation
- 3) pH change
-
Denaturation
- Temporary change of a protein's shape/function
- Might resume shape after factor is removed
-
Coagulation
Permanent change to a protein's shape/function
-
What are catalysts?
Speed up the rate of reactions without being consumed (changed)
-
What are enzymes?p
Protein catalysts that permit low temperature reactions by reducing the activation energy (energy makes things happen).
-
How are enzymes named after they bind with substrates?
Most enzyme names end with "ase"
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Parts of an enzyme and their description.
- 1) Active site: Site of reaction
- 2) Substrate: Substance changed by enzyme, can be split or built (cata/anabolic)
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Induced fit model
Enzyme active site squeezes down onto a specific substrate (1 enzyme for 1 substrate)
-
Cofactors
- Inorganic molecules
- - Bind to an enzyme to "activate" it
-
Coenzyme
- Organic molecules (from vitamins)
- - Bind to adjust the active site to receive the substrate
-
What 4 things affect an enzyme's activity?
- - pH level
- - Substrate concentration
- - Enzyme concentration
- - Temperature change
- - Competitive inhibitors
-
What happens to an enzyme when the pH level changes?
Denatured or becomes not as efficient
-
What is the effect of substrate concentration on enzyme activity?
The increased number of substrates increases collisions, and therefore reactions, until no more enzymes are available.
-
What is the optimum temperature for human enzymes?
35° - 40°C (95° - 104°F)
-
What happens to an enzyme at:
1) Low temperatures
2) As the temperature increases?
3) At very high temperatures?
- 1) Molecules move slowly
- 2) Molecules move faster and reaction rates increases
- 3) Enzyme structure is denatured
-
Competitive inhibitors
Competes for active site and mimics the substrate (renders enzyme useless)
-
Allosteric activity
Enzyme activity (its doing something)
-
Feedback inhibition
- Final product of a metabolic pathway, inhibits future production.
- "Off switch"
-
Precursor activity
- Activating of the last enzyme by the initial reaction in the metabolic pathway, speeds up reactions.
- "On Switch"
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