7.1 Study Guide Flashcards

1
Q

Cutting and joining the molecules of life

A

Enymes

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2
Q

Getting back and forth across the membrane

A

Pumps, channels, receptors

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3
Q

Engaging in constant battle in the bloodstream

A

Antibodies

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4
Q

Supporting and moving cells

A

Infrastructure

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5
Q

Carrying molecular messages through the blood

A

Hormones

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6
Q

Tertiary structure (hydrophobic interaction)

A

Fold into middle of protein

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7
Q

Tertiary structure (hydrophillic interaction)

A

Fold towards outside of protein

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8
Q

Tertiary structure (acidic and basic interaction)

A

Attract to each other due to opposite charges (ionic bond)

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9
Q

Tertiary structure (cysteine interaction)

A

Forms covalent disulfide bonds

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10
Q

A small organic compound having an amino group, a carboxylic acid group, a hydrogen atom, and an R group

A

Amino acid

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11
Q

A coiled or pleated pattern of protein structure caused by regular intervals of H bonds

A

Secondary structure

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12
Q

Hemoglobin, a globular protein of four chains is an example a protein with this

A

Quaternary structure

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13
Q

Folding of protein through interactions among R groups of a polypeptide chain

A

Tertiary structure

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14
Q

Type of covalent bond linking one amino acid with another

A

Peptide bond

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15
Q

Breaking weak bonds in large molecules (such as proteins) to change it shape so it no longer functions

A

Denaturation L

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16
Q

Lowest level of protein structure; has a linear, unique sequence of amino acids

A

Primary structure

17
Q

What makes amino acids polar

A

Polar functional group(s)
Ex: OH, COOH, SH

18
Q

What makes amino acids acidic

A

COOH- group

19
Q

What makes amino acids basic

A

NH3+ group

20
Q

What makes amino acids nonpolar

A

Contains C-H, symmetrical

21
Q

Polar functional groups

A

OH, SH, CO

22
Q

Acidic functional groups

A

COOH-

23
Q

Basic functional groups

A

NH3+

24
Q

Nonpolar functional groups

A

CH3