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CAU > cell biology 1 > Flashcards

cell biology 1 Flashcards

1
Q

enzymes

A

function as catalysts, increasing the rates og chemical reactions

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2
Q

structural proteins

A

physical support and shape

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3
Q

motility proteins

A

contraction and movement

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4
Q

regulatory proteins

A

control and coordinate cell function

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5
Q

transport proteins

A

move substances in and out of cells

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6
Q

hormonal proteins

A

communication between cells

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7
Q

defensive proteins

A

protect against disease

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8
Q

storage proteins

A

reservoirs of amino acids

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9
Q

receptor proteins

A

enable cells to respond to chemical stimuli from the environment

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10
Q

how many amino acids used in protein synthesis?

A

20

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11
Q

which stereoisomer occur in proteins?

A

L-amino acid

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12
Q

dehydration / condensation reactions

A

Amino acids are linked together stepwise into a linear polymer by DEHYDRATION (or CONDENSATION) reactions

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13
Q

the end of polypeptide with the amino group

A

is called N (or amino) terminus

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14
Q

the end of the polypeptide with the carboxyl group

A

is called C (or carboxyl) terminus

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15
Q

protein synthesis

A

The process of elongating a chain of amino acids

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16
Q

conformation

A

protein proper shape

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17
Q

both covalent bonds and noncovalent interactions are needed for a protein to

A

adopt its proper shape

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18
Q

bonds in protein

A

disulfide bond
hydrogen bond
ionic bond
Van der Waals and hydrophobic interactions

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19
Q

covalent disulfide bonds

A

They form through the removal of two hydrogen ions (oxidation) and can only be broken by the addition of two hydrogens (reduction)

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20
Q

intramolecular disulfide bonds

A

form between cysteines in the same polypeptide

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21
Q

intermolecular disulfide bonds

A

form between cysteines in two different polypeptides

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22
Q

noncovalent bonds and interactions

A

hydrogen and ionic bonds, and van der Waals, and hydrophobic interactions
these are individually weaker than covalent bonds but collectively can strongly influence protein structure and stability

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23
Q

donors

A

hydroxyl groups of several amino acids

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24
Q

acceptors

A

carbonyl or sulfhydryl groups

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25
Q

ionic bonds

A

electrostatic interactions
form between positively and negatively charged R groups
Because they depend on the charge on the R groups, changes in pH can disrupt ionic bonds

26
Q

four levels of organization in the protein

A

primary structure - amino acid sequence
secondary structure - local folding of polypeptide
tertiary structure - three-dimensional confirmation
quaternary structure - interactions between monomeric proteins to form a multimeric unit

27
Q

primary structure

A

amino acid sequences are written from the N-terminus to the C-terminus
primary structure is important genetically because the sequence is specified by the order of nucleotides in the corresponding messenger RNA

28
Q

secondary structure

A

describes local regions of structure that result from hydrogen bonding between NH and CO groups along the polypeptide backbone
These result in two major patterns, the alfa helix and the beta sheet

29
Q

alfa helix

A

spiral shape
A hydrogen bond forms between the NH group of one amino acid and the CO group of a second amino acid that is one turn away from the first

30
Q

beta sheet

A

extended sheetlike conformation with successive atoms of the polypeptide chain located at “peaks” or “troughs”

31
Q

motifs

A

Examples include the beta-alfa-beta, the hairpin loop (beta-beta), and the helix-turn-helix motifs (alfa-alfa)

32
Q

tertiary structure

A

The tertiary structure reflects the unique aspect of the amino acid sequence because it depends on interactions of the R groups

33
Q

native conformation

A

The most stable possible three-dimensional structure of a particular polypeptide

34
Q

proteins can be divided into two broad categories

A

fibrous proteins
globular proteins

35
Q

fibrous proteins

A

have extensive regions of secondary structure, giving them a highly ordered, repetitive structure

36
Q

glovular proteins

A

folded into compact structures

37
Q

domain

A

is a discrete locally folded unit of tertiary
structure, usually with a specific function

38
Q

quaternary structure

A

the bonds and forces maintaining quaternary structure are the same as those responsible for tertiary structure
sometimes molecular chaperones are required to assist the process

39
Q

nucleic acids

A

store, transmit, express genetic information

40
Q

DNA

A

deoxyribonucleic acid

41
Q

RNA

A

ribonucleic acid

42
Q

RNA synthesis

A

transcription
mRNA export
translation (takes place in cytoplasm)

43
Q

purines

A

adenine
guanine

44
Q

pyrimidines

A

thymine
uracil
cytosine

45
Q

in nucleic acids nucleotides are linked by

A

3’,5’ phosphodiester bridge

46
Q

nucleotide sequences are conventionally written in the

A

5’ to 3’ direction

47
Q

complementary base pairing

A

A - - T
G - - - C

48
Q

polysaccharides

A

long chain polymers of sugars and sugar derivatives that are not informational molecules

49
Q

aldosugars

A

terminal carbonyl group

50
Q

ketosugars

A

internal carbonyl group

51
Q

glucose

A

aldohexose D-glucose (C6H12O6)
DDDDDDDDD most stable form of glucose

52
Q

alfa D glucose

A

hydroxyl group downward

53
Q

beta D glucose

A

hydroxyl group upward

54
Q

storage polysaccharides

A

starch - plant cells
glycogen - animal cells
Both consist of -D-glucose units linked by - glycosidic bonds, involving carbons 1 and 4 (1→4)

55
Q

cellulose

A

composed of repeating monomers of beta-D-glucose

56
Q

lipids

A

hydrophobic nature
functions include energy storage, membrane structure, or specific biological functions such as signal transmission

57
Q

fatty acids

A

the polar carboxyl group is the “head” and the nonpolar hydrocarbon chain is the “tail”

58
Q

saturated fatty acids

A

no double bonds, pack together well
solid at room temperature

59
Q

unsaturated fatty acids

A

one or more double bonds, so have bends in the chains and less tight packing
liquid at room temperature

60
Q

phosphoglycerides

A

are the predominant phospholipids in most membranes

61
Q

sphingolipids

A

are basedon the amine sphingosine, which has a long hydrocarbon chain with a single site of unsaturation near the polar end

CAU (17 decks)

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