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1

polymers of nucleotides that store, transmt and express hereditary/genetic info. two types: DNA and RNA

nucleic acids

1

free energy

the amount of energy in a system that is available to do work

1

DNA sequence that makes specific proteins

gene

1

homeostasis

maintaining internal condition (such as pH, body temp)

2

transcription

after DNA replication, DNA sequences (of bases) being copied into RNA

2

biological catalysts. all are proteins. always end in "-ase". work by inducing strain or changing orientation of substrate or adding a chemical group

enzyme

2

gene expression

base sequences are copied from DNA to RNA to specify amino acid sequences in protein

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RNA

temporary molecule that can be modified, has OH instead of H so it can be more reactive. single stranded. can fold according to base pairs. info from DNA is transmitted through these to specifcy amino acid sequences of protein

4

proteins

these are macromolecules. polymers made out of amino acids. They govern chemical reactions in cells and form organism’s structure. Functions include enzymes, receptor, transport and genetic regulation

4

active site

location on the enzyme where the substrates bind to. it has specifc shape and chemical properties so not any molecule can bind there

5

after DNA replication, DNA sequences (of bases) being copied into RNA

transcription

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polypeptides

longer polymers of peptides with a unique sequence of amino acids. another word for protein

7

quaternary structure

results from subunites (2+ polypeptide chains binding together). not in al proteins

7

longer polymers of peptides with a unique sequence of amino acids. another word for protein

polypeptides

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covalent bond that connects phosphate to 3' carbon (pentose sugar) to link nucleotides. formed from condensation reactions

phosphodiester bond

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a molecule that binds noncovalently to the enzyme's active site and blocks the natural substrate. it is reversible

competitive inhibitor

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the amount of energy in a system that is available to do work

free energy

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enzyme

biological catalysts. all are proteins. always end in "-ase". work by inducing strain or changing orientation of substrate or adding a chemical group

11

noncompetitive inhibitor

molecule that binds to an enzyme at a site other than the active site. it causes a change in the shape of the enzyme which alters its activity. the substrate may no longer bind to the active site. if it does, it is reduced. this is reversible. this is a type of allosteric regulation

12

ions or molecules that some enzymes require in order to function. e.g. metal ions, coenzymes or prosthetic groups

cofactors

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molecule that binds to an enzyme at a site other than the active site. it causes a change in the shape of the enzyme which alters its activity. the substrate may no longer bind to the active site. if it does, it is reduced. this is reversible. this is a type of allosteric regulation

noncompetitive inhibitor

13

beta pleated sheets

interactions between a bunch of R groups. 2+ polypeptide bonds extended. flat portion of potein

15

alpha helix

in secondary structure of potein. right handed coil/ helix

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DNA

polymer of nucleotide subunits (A, T, G, C). stores and transmits genetic info. double stranded. strands run in opposite directions and form a ladder that twists into a double helix. lacks OH group so it is more table. made of pentose sugar, base and phosphate. phosphate and sugar are stable

17

primary structure of a protein

sequence of amino acids

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nucleotide sequence (of bases) in RNA specify sequences of amino acids in proteins

translation

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isozymes

enzymes which catalyze the same reaction with different chemical composition and physical properties. can catalyze at different pH/temp. this allows organisms to adapt to changes in the environment

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enzymes which catalyze the same reaction with different chemical composition and physical properties. can catalyze at different pH/temp. this allows organisms to adapt to changes in the environment

isozymes

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feedback inhibition

when an end product has high concentration, it binds to the commitment step (first) enzyme to make it inactive. binds to either the active site or allosteric site (not active site).

22

when a non-substrate molecule binds/modifies a site other than the active site of an enzyme. this causes the enzyme to change its shape and changes the rate of reaction or prevents substrate from entering active site. it can also activate an inactive enzyme. types include noncompetitive inhibitor and protein kinases

allosteric regulation