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| an organic molecule with only carbon and hydrogen. They are hydrophobic |
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| A variation in an organic compound with different structures and therefore different properties |
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| isomers with different arrangements of atoms and covalent arrangements |
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| Have the same covalent partnerships but different spatial arrangements |
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| Molecules that are mirror images of each other |
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| components of organic molecules that are commonly involved in chemical reactions |
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| H is bonded to an O in the carbon skeleton. |
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| Things that contain compounds from the hydroxyl |
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| CO has carbon joined to an oxygen atom with a double bond. |
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| A carbonyl at the end of a carbon chain |
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| A carbonyl to not at the end of a carbon chain |
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| An organic compound with a carbonyl and hydroxyl coming off of one carbon. Acidic from the hydroxyl O-/H+ equilibrium. |
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| Things in the amino group |
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| Organic molecules possessing both carboxyl and amino groups. Also, at the bottom, they have a variable group symbolized by R. This R group differentiates the various amino acids. 20 can be used by humans |
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| Things in the sulfhydryl group |
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| Things with OPO3 ^2- Comes from the phosphoric acid (H3PO4). Functions in this group transfer energy between organic moleucles. |
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| The totality of an organism's chemical reactions. It's like a cell road map of chemical reactions arranged intricately. It manages the energy and resources of a cell. |
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| When the breaking down of complex molecules to simpler molecules releases energy |
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| When sugar glucose and other organic fuels aer broken down to carbon dioxide and water. This is a catabolic process. |
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| Processes that consume energy to build complicated molecules from smaller ones. For example, the synthesis of a protein to amino acids |
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| The study of how organisms manage their energy resources |
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| The energy stored in molecules as a result of the arrangement of atoms in those molecules. |
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| The study of energy transformations |
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| When something is isolated from its surroundings |
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| Energy that can be transferred between the system and the surroundings |
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| Ist law of thermodynamics |
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| A law that says the energy of the universe is constant. It can be transformed, but never created or destroyed |
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| 2nd law of thermodynamics |
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| A law that says every energy tansformation makes the universe disorderly. |
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| The disorderliness of the universe |
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| The portion of a system's energy that can perform work when temperature is unifrom throughout the system. |
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| Free energy = the total energy of a system - temperature (in K) x Enrtopy. G = H - TS |
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| A system that gives up energy (- G |
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| Has a net release of energy. Spontaneous |
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| A reaction that absorbs free energy |
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| Something in equilibrium cannot do work. For metabolism, this is a vital process |
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| Three types of work a cell does |
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| Mechanical work (moving stuff), transport work (moving shit against the current), and chemical work, endergonic work that needs energy to get done. |
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| Adenosine triphosphate. A molecule with three phosphate groups, one ribose group, and an adenine group (an NH2 group.) The ATP is used in energy coupling a lot. A terminal phosphate is broken off due to hydrolysis. The ATP becomes ADP, and the endergonic reaction is given energy to react. Once the reaction happens, the P is let go and solar energy reconnects the ADP to the P making it ATP. |
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| A chemical agent that changes the rate of reactions without being consumed by the reaction. |
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| What an enzyme reacts to. Each enzyme only fits with a certain substrate |
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| What effects an enzyme's rate of reaction? |
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| The rate at which a given amount of enzyme converts into a substrate is relevant to how much of a substrate there is. |
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| Once there is enough of a substrate for an enzyme to be always finding an active site, adding more substrate won't make it go faster. |
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| Usually 6-8, but there are some exceptions |
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| Non-protein catalytic activators. They are inorganic and either take up permanent residence in the active site or are loose and reversible in that area |
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| Non-protein catalytic activators that are organic. |
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| Things that inhibit the areas in which enzymes would usually be. They prevent enzymes from entering their substrates. They can be reversible with weak bonds, or irreversible with strong bonds. |
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| Reduce the production of enzymes by entering their sites |
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| Noncompetitive inhibitors |
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| An inhibitor that goes into another part of the enzyme causing the activation site to change shape and not let the enzyme in. |
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| Condensation reaction/Dehydration reaction |
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| A reaction in which monomers connect in a reaction to each other via a loss of water |
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| A process in which molecules connect to each other. |
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| Sugar monomers that are generally divisible by CH2O. It ranges from three to seven carbons long and end in -ose. |
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| A sugar that consists of two or more monosaccharides. |
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| A covalent bond that formed between two monosaccharides by a dehydration reaction. |
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| Macromolecules with a few hundred to a few thousand monosaccharides joined by glycosidic linkages |
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| A polymer consisting entirely of glucose monomers (alpha.) It stores a lot of energy. |
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| A polysaccharide of glucose with different ring of glucose (beta glucose) |
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| A macromolecule constructed from two kinds of smaller molecules: glycerol and fatty acids. Glycerol is an alcohol with three carbon chains. A fatty acid has a long carbon skeleton (16-18 carbons in length.) At one end of the fatty acid is a carboxyl group and it connects to the glycerol via a glycosidic linkage. |
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| A fat without a double bond between any of the carbons on the carbon skeleton |
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| A fat with a double bond between one of the carbons in the carbon chain. |
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| Fats with two acid tails rather than three and glycerol linkage to a phosphate group and a choline. They have a hydropphilic head and a hydrophobic tail. |
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| Lipids characterized by a skeleton of four fused rings. |
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| A common component of animal cells that synthesizes many hormones and such. |
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| One of more polypeptides folded and coiled into specific conformations |
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| The bond made when two amino acids are positioned so that the carboxyl group of one is adjacent to the amino group of the other an enzyme can cause them to join by catalyzing dehydration reaction. |
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| The sequence of a protein's amino acids. |
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| The shape of the coils and folds of the polypeptide chains. |
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| a coild held together hydrogen bonds |
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| When two or more regions lie parallel to each other |
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| Due to interactions of different parts of the molecules between each other to shape it |
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| The effects of linked polypeptide chains |
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| The switching of a metabolic pathway by its end product whcich acts as an inhibitor enzyme iwhin the pathway |
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| When an enzyme has two or more subunits and a substrate triggers the same favorable confromational change in all the subunits. |
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| An active site which moves from being open to an activator and being closed, all due to the presence of an enzyme (or an inhibitor to keep it from moving to an activator friendly state |
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| carbohydrate, lipid, protein, nucleic acid |
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