Chapter 3 Flashcards

(66 cards)

1
Q

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

A

nucleic acids

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1
Q

free energy

A

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

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1
Q

DNA sequence that makes specific proteins

A

gene

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1
Q

homeostasis

A

maintaining internal condition (such as pH, body temp)

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2
Q

transcription

A

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

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2
Q

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

A

enzyme

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2
Q

gene expression

A

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

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3
Q

RNA

A

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

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4
Q

proteins

A

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

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4
Q

active site

A

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

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5
Q

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

A

transcription

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7
Q

polypeptides

A

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

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7
Q

quaternary structure

A

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

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7
Q

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

A

polypeptides

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8
Q

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

A

phosphodiester bond

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8
Q

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

A

competitive inhibitor

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9
Q

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

A

free energy

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10
Q

enzyme

A

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

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11
Q

noncompetitive inhibitor

A

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

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12
Q

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

A

cofactors

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12
Q

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

A

noncompetitive inhibitor

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13
Q

beta pleated sheets

A

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

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15
Q

alpha helix

A

in secondary structure of potein. right handed coil/ helix

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16
Q

DNA

A

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

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17
primary structure of a protein
sequence of amino acids
18
nucleotide sequence (of bases) in RNA specify sequences of amino acids in proteins
translation
19
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
20
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
21
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
23
peptide bonds
covalent bond links together amino acids to form protein. condensation reactions links amino group of the new amino acid chain with the carboxyl group of the amino acid at the end of the chain
24
denatured
caused by change in temp, pH, polar/nonpolar substance, the heat energy will disrupt the weaker interactions causing the secondary and tertiary structure to break down
25
induced fit
enzyme changes active site to fit substrate
27
nucleic acids
polymers of nucleotides that store, transmt and express hereditary/genetic info. two types: DNA and RNA
27
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
DNA
28
location on the enzyme where the substrates bind to. it has specifc shape and chemical properties so not any molecule can bind there
active site
29
catalyst
speeds up a reaction by lowering activation energy required (by enabling reactants to come togher and react more easily) without being permanently altered. e. g. enzyme
31
secondary structure
regular, repeated patterns in the polypeptide chain. two types (alpha helix and beta pleated sheet) determined by hydrogen bonding between amino acids. held together by hydrogen bonds
32
base sequences are copied from DNA to RNA to specify amino acid sequences in protein
gene expression
33
results from subunites (2+ polypeptide chains binding together). not in all proteins
quaternary structure
34
gene
DNA sequence that makes specific proteins
36
translation
nucleotide sequence (of bases) in RNA specify sequences of amino acids in proteins
38
purine
type of base with double rings. A, G
40
speeds up a reaction by lowering activation energy required (by enabling reactants to come togher and react more easily) without being permanently altered. e. g. enzyme
catalyst
42
sequence of amino acids
primary structure of a protein
43
type of base with double rings. A, G
purine
44
maintaining internal condition (such as pH, body temp)
homeostasis
45
pyrimidines
type of base with single rings. C, T, U
47
cofactors
ions or molecules that some enzymes require in order to function. e.g. metal ions, coenzymes or prosthetic groups
48
enzyme changes active site to fit substrate
induced fit
50
competitive inhibitor
a molecule that binds noncovalently to the enzyme's active site and blocks the natural substrate. it is reversible
52
phosphodiester bond
covalent bond that connects phosphate to 3' carbon (pentose sugar) to link nucleotides. formed from condensation reactions
53
reactants in an enzyme-catalyzed reaction. they bind to the active site on the enzyme
substrates
54
substrates
reactants in an enzyme-catalyzed reaction. they bind to the active site on the enzyme
55
in secondary structure of potein. right handed coil/ helix
alpha helix
56
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
RNA
57
type of base with single rings. C, T, U
pyrimidines
58
caused by change in temp, pH, polar/nonpolar substance, the heat energy will disrupt the weaker interactions causing the secondary and tertiary structure to break down
denatured
58
allosteric regulation
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
60
tertiary structure of protein
polypeptide chain is bent and folded to form 3D shape. the outersurfaces have functional groups capable of interacting with other molecules in the cell. determined by interaction between R groups
61
regular, repeated patterns in the polypeptide chain. two types (alpha helix and beta pleated sheet) determined by hydrogen bonding between amino acids. held together by hydrogen bonds
secondary structure
62
covalent bond links together amino acids to form protein. condensation reactions links amino group of the new amino acid chain with the carboxyl group of the amino acid at the end of the chain
peptide bonds
63
interactions between a bunch of R groups. 2+ polypeptide bonds extended. flat portion of potein
beta pleated sheets
64
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
proteins
65
polypeptide chain is bent and folded to form 3D shape. the outer surfaces have functional groups capable of interacting with other molecules in the cell. determined by interaction between R groups
tertiary structure of protein
66
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).
feedback inhibition