Unit 4 Flashcards

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1
Q

________ structure level of proteins: order of amino acids.

A

Primary

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2
Q

_________ structure level of proteins: small spirals or kinks.

A

Secondary

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3
Q

______ structure level of proteins: polypeptide folds into globular structure.

A

Tertiary

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4
Q

________ structure level of proteins: combination of multiple polypeptides

A

Quaternary

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5
Q

not all proteins have every level, many lack _____ and _______.

A

Tertiary and Quaternary

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6
Q
  • Guide proper folding.
  • Reduce aggregation.
A

Chaperonin

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7
Q

______ of proteins can lead to disease and allergies.

A

misfolding

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8
Q

_______ is when a protein unfolds and loses its secondary, tertiary, quaternary structure.

A

Denaturation

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9
Q

how can cells use denaturation

A

to turn proteins on or off

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10
Q

Biological catalysts

A

Enzymes

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11
Q

long chain of amino acids linked by peptide (covalent) bonds

A

Polypeptides

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12
Q

determines the amino acid’s nature (that is, whether it is acidic, basic, polar, or nonpolar)

A

Side Chain or R group

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13
Q

energy necessary for a reaction to occur

A

Activation energy

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14
Q

Molecule on which enzymes act

A

substrate

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15
Q

the region of an enzyme where a substrate binds

A

Active site

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16
Q

Molecule that activates enzymes

A

Cofactor

17
Q

What are the two types of cofactors?

A

o Inorganic cations
o Coenzymes = organic molecules (often vitamins)

18
Q

molecule that inactivates enzyme.

A

Inhibitor

19
Q

______ inhibitors bind at active site and blocks active site

A

competitive

20
Q

______ inhibitors bind away from active site. – change shape of active site.

A

non-competitive

21
Q

molecule increases or decreases enzyme activity by binding away from active site.

A

allosteric regulator