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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
ionic bonds
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
four levels of organization in the protein
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
primary structure
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
secondary structure
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
alfa helix
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
beta sheet
extended sheetlike conformation with successive atoms of the polypeptide chain located at “peaks” or “troughs”
31
motifs
Examples include the beta-alfa-beta, the hairpin loop (beta-beta), and the helix-turn-helix motifs (alfa-alfa)
32
tertiary structure
The tertiary structure reflects the unique aspect of the amino acid sequence because it depends on interactions of the R groups
33
native conformation
The most stable possible three-dimensional structure of a particular polypeptide
34
proteins can be divided into two broad categories
fibrous proteins globular proteins
35
fibrous proteins
have extensive regions of secondary structure, giving them a highly ordered, repetitive structure
36
glovular proteins
folded into compact structures
37
domain
is a discrete locally folded unit of tertiary structure, usually with a specific function
38
quaternary structure
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
nucleic acids
store, transmit, express genetic information
40
DNA
deoxyribonucleic acid
41
RNA
ribonucleic acid
42
RNA synthesis
transcription mRNA export translation (takes place in cytoplasm)
43
purines
adenine guanine
44
pyrimidines
thymine uracil cytosine
45
in nucleic acids nucleotides are linked by
3',5' phosphodiester bridge
46
nucleotide sequences are conventionally written in the
5' to 3' direction
47
complementary base pairing
A - - T G - - - C
48
polysaccharides
long chain polymers of sugars and sugar derivatives that are not informational molecules
49
aldosugars
terminal carbonyl group
50
ketosugars
internal carbonyl group
51
glucose
aldohexose D-glucose (C6H12O6) DDDDDDDDD most stable form of glucose
52
alfa D glucose
hydroxyl group downward
53
beta D glucose
hydroxyl group upward
54
storage polysaccharides
starch - plant cells glycogen - animal cells Both consist of -D-glucose units linked by - glycosidic bonds, involving carbons 1 and 4 (1→4)
55
cellulose
composed of repeating monomers of beta-D-glucose
56
lipids
hydrophobic nature functions include energy storage, membrane structure, or specific biological functions such as signal transmission
57
fatty acids
the polar carboxyl group is the “head” and the nonpolar hydrocarbon chain is the “tail”
58
saturated fatty acids
no double bonds, pack together well solid at room temperature
59
unsaturated fatty acids
one or more double bonds, so have bends in the chains and less tight packing liquid at room temperature
60
phosphoglycerides
are the predominant phospholipids in most membranes
61
sphingolipids
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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