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Biology 243 > Topic 2C > Flashcards

Topic 2C Flashcards

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1
Q

what determines a protein’s shape and function?

A

the exact order of amino acids

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2
Q

what does an amino acid molecule consist of?

A

an alpha carbon (central), an amino group (NH2), a carboxyl group (COOH) and a side chain/R group

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3
Q

at cellular pH, what happens to the amino acid molecule?

A

amino group gains a proton (NH3+) and carboxyl group loses a proton (COO-)

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4
Q

what shape is an amino acid?

A

tetrahedron

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5
Q

what determines the amino acid’s different chemical/physical properties?

A

the R group

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6
Q

how does the R group determine the structures of the protein?

A

it influences how a polypeptide fold and hence the 3D shape and properties of a protein

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7
Q

what do hydrophobic amino acids consist of?

A

nonpolar R groups composed of hydrocarbon chains or uncharged carbon rings

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8
Q

where are most hydrophobic amino acids located?

A

in the interior of folded proteins (away from water)

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9
Q

amino acids with polar R groups tend to form…

A

hydrogen bonds with each other or with water molecules (hydrophilic)

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10
Q

where are charged R groups of amino acids located?

A

on the outside surface of a folded molecule

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11
Q

peptide bond

A

a covalent bond that links the carbon atom in the carboxyl group of one amino acid to the nitrogen atom in the amino group of another amino acid

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12
Q

amino end

A

the end of a polypeptide chain that has a free amino group

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13
Q

carboxyl

A

the end of a polypeptide chain that has a free carboxyl group

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14
Q

polypeptide

A

a polymer of amino acids connected by peptide bonds

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15
Q

protein

A

the key structural and functional molecules that do the work of the cell, providing structural support and catalyzing chemical reactions. The term “protein” is often used as a synonym for “polypeptide”

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16
Q

residue

A

any of the amino acids that is incorporated into a protein

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17
Q

primary structure

A

the sequence of amino acids in a protein

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18
Q

secondary structure

A

the structure formed by interactions between stretches of amino acids in a protein

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19
Q

tertiary structure

A

The overall three-dimensional shape of a protein, formed by interactions between secondary structures.

20
Q

quaternary structure

A

The structure that results from the interactions of several polypeptide chains.

21
Q

secondary structure results from

A

hydrogen bonding in the polypeptide backbone

22
Q

what are the two types of secondary structure found in proteins?

A

alpha helix and beta sheet

23
Q

tertiary structures result from

A

interactions between amino acid side chains

24
Q

denaturation

A

the unfolding of proteins by chemical treatment or high temperature

25
Q

chaperone

A

a protein that helps shield a slow-folding protein until it can attain its proper three-dimensional structure

26
Q

translation

A

synthesis of a polypeptide chain corresponding to the coding sequence present in a molecule of messenger RNA

27
Q

messenger RNA (mRNA)

A

the RNA molecule that combines with a ribosome to direct protein synthesis; it carries the genetic “message” from the DNA to the ribosome

28
Q

ribosome

A

a complex structure of RNA and protein, bound to the cytosolic face of the RER in the cytoplasm, on which proteins are synthesized

29
Q

what are the three binding sites for tRNA on the large subunit of a ribosome?

A

animoacyl (A) site, peptidyl (P) site, and exit (E) site

30
Q

codon

A

a group of three adjacent nucleotides in RNA that specifies an amino acid in a protein or that terminates polypeptide synthesis

31
Q

reading frame

A

following a start codon, a consecutive sequence of codons for amino acids

32
Q

anticodon

A

the sequence of three nucleotides in a tRNA molecule that base pairs with the corresponding codon in an mRNA molecule

33
Q

what is the nucleotide sequence for each tRNA on its 3’ end?

A

CCA

34
Q

where does the corresponding amino acid to the anticodon on tRNA attach?

A

the 3’ hydroxyl of the A in CCA sequence on 3’ end

35
Q

aminoacyl tRNA synthetase

A

an enzyme that attaches a specific amino acid to a specific tRNA molecule

36
Q

genetic code

A

the correspondence between codons and amino acids, in which 20 amino acids are specified by 64 codons

37
Q

What was Khorana’s experiment?

A

using synthetic RNAs of known sequence to decipher the standard genetic code

38
Q

initiation

A

the stage of translation in which methionine is established as the first amino acid in a new polypeptide chain

39
Q

elongation

A

the process in protein translation in which successive amino acids are added one by one to the growing polypeptide chain

40
Q

termination

A

in protein translation, the time at which the addition of amino acids stops and the completed polypeptide chain is released from the ribosome.

41
Q

initiation factor

A

a protein that binds to mRNA to initiate translation

42
Q

elongation factor

A

a protein that breaks the high-energy bonds of the molecule GTP to provide energy for ribosome movement and elongation of a growing polypeptide chain

43
Q

release factor

A

a protein that causes a finished polypeptide chain to be freed from the ribosome

44
Q

describe translation initiation in eukaryotes:

A

initiation complex forms at the 5’ cap and scans along the mRNA until the first AUG is encountered

45
Q

describe translation initiation in prokaryotes:

A

the mRNA molecules have no 5’ cap, initiation complex is formed at one or more internal sequences present in the mRNA known as a Shine-Dalgarno sequence

46
Q

polycistronic mRNA

A

a single molecule of messenger RNA that is formed by the transcription of a group of functionally related genes located next to one another along bacterial DNA

47
Q

operon

A

a group of functionally related genes located in tandem along the DNA and transcribed as a single unit from one promoter; the region of DNA consisting of the promoter, the operator, and the coding sequence for the structural genes

Biology 243 (15 decks)

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