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| diverse group of water-insoluable mosly nonpolar biological molecules composed mostly of hydrocarbons |
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| called energy storage molecules. they are neutral because at cellular PH they have no charged groups. They are therefore non polar |
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| examples of neutral lipids |
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| oils are what at bilogical temperature |
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| fats are what at bioogical temperature |
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| contains a single hydrocarbon chain with a carboxyl group (-COOH) at one end |
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| when a hydrocarbon chain of fatty acid binds the maximum possible number of hydrogen atoms, so only single bonds link the carbon atoms |
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| if one or more double bonds link the carbons reducing the number of carbon atoms bound |
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| fatty acids with one double bond |
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| fatty acids with more than one double bond |
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| unsaturated fatty acid chains tend to what at the double bond? |
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| adding hydrogen atoms to increase the degree of saturation |
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| the primary lipids of cell membranes |
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| group of lipids with structures based on a framework of 4 carbon rings |
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| if a fatty acid binds a dehydration synthesis at each of glycerols three-OH bering sites, the polar groups are eliminated, producing a non polar compound |
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| is an important component of the boundary membrane surrounding animal cells |
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| a molecule that contains both an amino and a carboxyl group |
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| is formed by a dehydration synthesis reaction between the NH2 group of one amino acid of the COOH group of a second |
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| an amino acid chain always has an NH2 group (NH3 in ionized form) at one end |
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Definition
| has a COOH group (COO- in ionized form) at the other end |
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| has a COOH group (COO- in ionized form) at the other end |
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| a chain of amino acids formed by sequential peptide bonds |
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| primary structure of a protein |
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| is the particular and unique sequence of amino acids forming a polypeptide |
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| is produced by the twists and turns of the amino acid chain |
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| is the folding of the amino acid chain with its secondary structures, into the overall three-demensial shape of a protein. |
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| primary secondary and tertiary structures |
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| the arrangement of polypeptide chains in a protein that is formed from more than one chain |
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| it is the backbone of the amino acid chain which is twisted into a regular right hand spiral |
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| b strands are aligned side by side in the same or opposite directions to form a structure known as a beta sheet |
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| the amino acid chain has an irregularly folded arrangement |
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| the tertitary structure of a protein is its overall three dimensional shape |
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| unfolding a protein from its active conformation so that it loses its structure and function |
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| the reversal of denaturation |
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| or known as guide proteins. they bind temporarily with newly synethesised proteins, directing their conformation toward the correct tertiary structure and inhibiting incorrect arrangements as the new proteins fold. |
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| the tertituary structureof most proteins is flexible allowing them to undergo limited alterations in three demential shapes |
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Definition
| folding of amino acid chains produces distinct large structural subdivisions |
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| three dimensional arrangement of amino acid chains within and between domains also produces highly specialized regions |
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| what are the 2 types of nucleic acids? |
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| stores the heriditary information responsible for inherited traits in all eukaryotes and prokaryotes ina large group of viruses |
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| is the heriditary molecule of another large group of viruses in all organisms, one major type of RNA carries the instructions for assembling proteins from DNA to the sites where proteins are made inside cells |
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| the monomer of nucleic acids |
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| nucleotides consist of what three parts linked together by covalent bonds |
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| a nitrogeneous base, a five carbon ring shaped sugar, and one to three phosphate groups. |
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| formed from rings of carbon and nitrogen atoms |
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| what are 2 types of nitrogenous bases |
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| has 2 carbon nitrogen rings |
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| has one carbon nitrogen ring |
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| what are three pyrimindine bases |
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| uracil, thyamine, and cytosine |
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| deoxyribose and ribose are what |
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| is a structure containing only a nitrogenous base and a five carbon sugar |
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| DNA and RNA consist of chains of nucleotides, polynucleotide chains, with one nucleotide linked to the next by a bridging phosphate group between the 5 carbon of one sugar and and the 3 carbon of the next sugar inline |
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| who invented the double helix |
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Definition
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| consists of 2 nucleotide chains wrapped around each other in a spiral that resembles a twisted ladder |
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| in DNA replication one nucleotide chain is used as a template for the assembly of a complementary chain according to the A-T and G-C base pairing rules |
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| the biochemical modification and use of organic molecules and energy to support the activities of life |
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| is the energy of an object because it is in motion |
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| is stored energy which is the energy an object has because of its location or chemical structure |
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| the study of energy and its transformations |
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| what is the second law of thermodynamics |
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| states this tendency toward disorder formally in terms of a system and its surroundings: any process in which a system changes from its initial to final state |
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| predicting wheather any particular chemical of physical rxn will occur without the input of energy |
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| the potential energy in a system |
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| reactions that release energy |
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| reactions that absorb energy |
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| is one that releases free energy |
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| gains free energy from the surroundings |
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| energy is released by the breakdown of complex molecules into simpler compounds |
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| energy is used to build complicated molecules from simpler ones |
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Term
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| ATP comes into close contact with a reactant molecule involved in an endergonic reaction and when ATP is hydrolyzed the terminal phosphate group is transferred to the reactant molecule |
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Definition
| the addition of a phosphate group to a molecule |
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Definition
| the continual hydrolysis and resynethsis of ATP |
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Definition
| the initial energy investment required to start a reaction |
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| a chemical agent that accelerates the rate of a reaction without itself being changed by the reaction |
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| the process of accelerating a reaction with a catalyst |
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| the most common biological catalysts are proteins |
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| the reactant that an enzyme acts on |
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Definition
| each type of enzyme catalyzes the reaction of a single type of substrate molecule or a group of closely related molecules |
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Definition
| the place on the enzyme where catalysis occurs |
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| a nonprotein group that binds percisely to the enzyme for catalytic activity |
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| other cofactors which are small organic molecules. they are often derived from vitamins |
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Definition
| the inhibitor competes with the normal substrate for binding to the active site |
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| noncompetitive inhibition |
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Definition
| they bind to an enzyme at a location other than the active site |
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Definition
| when enzyme activity is controlled by the reversible binding of a regulatory molecule to the allosteric site |
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| a location on the enzyme outside the active site |
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| converts it from the low to high affinity state and therefore increases enzyme activity |
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| converts an allosteric enzyme from the high to low affinity state and therefore decreases enzyme activity |
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| the product of a reaction acts as a regulator of the reaction |
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| are RNA based catalysts which are part of the biological machinery of all cells |
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