EXAM 3 Lec 10 Flashcards

1
Q

enzymes

A

flexible and undergo staged shape changes during a catalytic reaction

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2
Q

what do the sequences of amino acids in proteins determine

A

the shape and potential noncovalent reactions

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3
Q

regulator molecules

A

change enzyme shape, affecting the activity of enzymes

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4
Q

primary structure

A

sequence of amino acids linked by peptide bonds
determines how the poly peptide interacts with itself and how it interactions with other proteins, ligands, and macromolecules.

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5
Q

secondary structure

A

nearby noncovalent interactions

hydrogen bonds in the polypeptide backbone create common folding patterns of alpha helices and beta sheets

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6
Q

tertiary structure

A

3-dimensional structure of one polypeptide
globular proteins are spherical (enzymes)
fibrous proteins are elongated (structural proteins)
includes secondary structures

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7
Q

quaternary structure

A

proteins where two or more polypeptides form a functional complex held together by noncovalent bonds
can form the same (CAP protein) or different (neuraminidase) polypeptides

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8
Q

how are proteins shaped and organized

A

by sequences of amino acids that contribute to shape and potential noncovalent interactions

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9
Q

how can protein shape be controlled

A

by molecules interacting with the protein
chemical modification of the amino acids
changes in the surrounding environment that affect noncovalent interactions (pH and temperature)

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10
Q

function of enzymes

A

bind a molecule, convert it to a different one, and then back to the original (bring 2 reactants close and redistribute their electrons)
they change their shape in an orderly process that favors product formation

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11
Q

what does the rate of a reaction include

A

the time the enzyme spends looking/binding to the substrate (dependent on substrate concentration of the enzyme), as well as the time spent converting it to a product

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12
Q

Vmax

A

time spent converting the substrate to a product

point of infinite concentration

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13
Q

reaction of the enzyme at low concentrations

A

the enzyme spends most time looking for the substrate, making the rate low

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14
Q

reaction of the enzyme at high concentrations

A

the enzyme spends less time looking or the substrate, increasing the rate

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15
Q

Km

A

one half Vmax

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16
Q

Q10

A

temperature coefficient

17
Q

effect of temperature on the rate of the reaction

A

temperature and activity increase together

continues increasing until the enzyme is heat-denatured

18
Q

enzyme shape guides substrates (reactants) towards

A

product formation

19
Q

how do enzymes affect a reactions energy

A

they reduce the amount of energy needed to start a reaction

20
Q

allosteric regulation

A

an enzyme has two sites for interacting with other compounds
the active site and the allosteric regulatory site

21
Q

active site

A

where the substrate binds and is converted into the product

22
Q

allosteric regulatory site

A

where another compound binds and affects the activity of the enzyme (usually a compound related to the metabolic pathway of the enzyme)