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Most common elements in organic molecules |
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Carbon, Hydrogen, Oxygen and Nitrogen |
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Unequal sharing of electrons resulting in a slightly positive and a slightly negative side of the molecule. Water is a polar molecule. |
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Thermal property of water |
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-Because of large heat capacity, water is thermally stable -Hydrogen bonding provides a means of storing P. + K. (Energy) Physiological use: -To prevent denaturation of enzymes water is used to cool body temp. -Maintains temp. due to heat capacity -Blood, which is mostly water, can carry away heat from hot to cooler parts Ecologically use: -Water bodies have fairly stable temp. |
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Cohesive property of water |
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Cohesion -> "sticking together b/w same molecule" Creates surface tension which is exploited by some insects |
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Solvent property of water |
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-Polar water molecules are attracted to the strong ionic charges of the ions in the solution -Often the ion (eg. Na(+)) exerts a strong enough attraction on water molecules that they form shells around the ion -This has the effect of isolating one ion from another which is essentially what is known as solubility. |
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Substance that cools temp. or acts as a heat sink absorbing heat. |
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Water is a transport medium allowing anything that has a charge or that is polar (like salts) to dissolve in it. This is why blood and cytoplasm is mostly composed of water. Water is a universal solvent. |
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Molecule that always contains carbon and hydrogen and often oxygen; organic molecules are associated with living things. |
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[image]Six-carbon sugar that organisms degrade as a source of energy during cellular respiration. -Monosaccharide -2 monosaccharides form one maltose |
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5 sided sugar -Monosaccharide [image] |
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Weak bond that arises b/w a slightly positive hydrogen atom of one molecule and a slightly negative atom of another molecule or b/w parts of the same molecule. |
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Monosaccharide (example/function) |
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Simple sugar; a carbohydrate that cannot be decomposed by hydrolysis eg. Glucose - Respiratory substrate |
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Sugar that contains two units of a monosaccharide eg. maltose - fundamental unit of glycogen |
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Polymer made from sugar monomers; the polysaccharides starch and glycogen are polymers of glucose monomers
eg. Glycogen - Insoluble storage polymer of glucose |
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Water insolube storage polysaccharide found in plants that is composed of glucose molecules joined in a linear fashion with side chains. The two types of glucose chains are called amylose and amylopectin. Typically there is 70-80% amylopectin and 20-30% amylose in starch. Amylopectin is a highly branched polymer made of A-glucose (1-4) bonds and branched with (1-6) bonds every 24-30 units. It is comparable to glycogen. Amylose is also made of A-(1-4)glucose molecules but has fewer (1,6) branches. |
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Storage polysaccharide, found in animals, that is composed of glucose molecules joined in a linear fashion but having numerous branches. Similar to amylopectin. |
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Polysaccharide composed of B-glucose molecules; the chief constituent of a plant's cell wall. |
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Splitting of a covalent bond by the addition of water so that it can provide an oxygen atom and a hydroxyl group. |
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Chemical reaction resulting in a covalent bond w/ the accompanying loss of a water molecule. |
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Organic compound that is insolube in water; notably fats, oils, and steroids. |
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Neutral fat composed of a glycerol and three fatty acids. |
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Backbone of a phospholipid, composed of a 3 carbon chain and 3 hydroxyl groups attached to it. |
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Fatty acid molecule that has one or more double bonds b/w the atoms of its carbon chain |
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Fatty acid molecule that lacks double bonds b/w the carbons of its hydrocarbon chain. The chain bears the maximum number of hydrogens. |
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Molecule that forms the bilayer of the cell's membranes; has a polar, hydrophillic phosphate group, and a nonpolar, hydrophobic fatty acid group |
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Amino Acid (Polar and Nonpolar) |
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Definition
Monomer of a protein; takes its name from the fact that it contains an amino group and an acid group Polar and non-polar amino acids allow for proteins to be embedded within the membrane. The sides of a protein will be non-polar (hydrophobic) and the corners and passage and corners will be polar(hydrophillic). |
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Polymer of many A.A. linked by a peptide bond. |
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Protein Structure (Primary, Secondary, Tertiary and Quaternary) |
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Definition
Primary- linear struct. of A.A. (Peptide bonds) Secondary- the tendency of the polypeptide to coil or pleat due to H-bonding b/w R-groups Tertiary- Controlled by bonding (or in some cases repulsion) b/w R-groups (Disulphate bonds) Quaternary- Formed from one or more polypeptides proteins, such as hemoglobin. Forming a globular protein. |
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-water insoluble -long and narrow -most common protein in animals -associated with providing strength and support to tissues eg. collagen - basis connective of tissue (comp. of 3 left-handed helices) |
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-near soluble (colloid) -more compact (rounded sphere-like) shape -functions as transport proteins such as hemoglobin, a catalytic(enzyme) like lactase, (immunoglobins) immune system eg. antibodies |
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Organic macromolecule that is composed of either one or several polypeptide |
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Covalent bond that joins two acids |
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Bases:(4 kinds are guanine, adenine, cytosine and thymine) -2 strands -Double helix |
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Deoxyribose sugar used in DNA- one less oxygen on carbon structure |
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3 parts : Phosphate, Sugar, Base Phosphate: (PO4 (-1))group Sugar: Ribose (RNA) Base:nitrogenous based ring structure (4 kinds are guanine, adenine, cytosine and uracil) |
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Definition
3 parts : Phosphate, Sugar, Base Phosphate: (PO4 (-1))group Sugar: Deoxyribose (DNA) Base:nitrogenous based ring structure (4 kinds are guanine, adenine, cytosine and thymine (DNA) and uracil (RNA)) -Nucleotides are covalentely bonded between the phosphate of one group and the c3 of the second nucleotide -Bases are joined by hydrogen bonds |
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1 ring: pyrimidine (DNA only) |
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A group that consists of Guanine and Adenine |
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A group that consists of Cytosine, Thymine and Uracil |
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Complementary base pairing |
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Definition
G will make a hydrogen bond with C A will make a hydrogen bond with T in DNA and a U in RNA |
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Parallel strands that go in opposite direction. 3' (3 prime) and 5'(prime) denote the direction the strand is going in. |
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-Globular -Speeds up biological reactions (catalysts) -unchanged by the reaction -specific to substrate |
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Position on the enzyme occupied by the substrate (binds to) |
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A model of an enzyme reaction that hypothesizes that enzymes only work on certain substrates because a specific shape is present among the substrates. These substrates then bind with the active site like a puzzle piece. |
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Enzyme specificity is due to the complimentary shape of the active site and another substrate. |
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The loss of shape and thus proper function in enzymes when they are subjected to innappropriate environments. |
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Effects of temp. on enzyme |
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-Increases rate of reaction but only to a point -Increase the KE of the substrate and enzyme ->more collisions of the substrate with the active site occur -However when heated too much the hydrogen bonds that give the enzyme its shape are destroyed. -Optimal temperature is the temp at highest rate of reaction |
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-Causes bonds to be created and be destroyed which changes the shape of the active site and decreases the rate of reaction -Optimal pH is the pH lvl at the highest rate of reaction |
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-As substrate concentration increases the reaction rate increases but to a point where it stops -This is because the enzymes cannot go any faster |
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A model of enzyme reaction that hypothesizes that an enzyme will change its shape after binding with the first substrate so that the binding of the second is easier. -When finished the product is ejected and the enzyme returns to its normal shape |
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-Energy req'd by the enzyme to perform the chemical reaction -Much less energy taken than without the enzyme |
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Spontaneous and realeases energy. |
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requires energy to initiate the reaction, the specific amount is called the activation energy |
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The use of lactase to reduce lactose found in milk into glucose and galactose. |
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sequence of enzymatic reactions where a substrate is changed from one molecule to another until the end product is formed |
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Enzyme inhibition that blocks the active site preventing any other reactions. |
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non-competitive inhibition |
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Definition
the substrate binds to the active site but slows the speed of the reaction |
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end-product inhibition (allosteric enzyme inhibition) |
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Definition
the substrate cannot bind to the active site because it is changed by the non-competitive inhibitor |
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