Amino Acids and Proteins Flashcards

1
Q

what are the 4 components of an amino acid

A
  1. carboxylic acid group
  2. variable R group
  3. hydrogen
  4. amino group
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2
Q

RNA virus

A

genetic material stored as RNA (not DNA)

genome can be used in host cell replication machinery and translated into proteins; or their RNA serves as a DNA-like template for protein translation

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3
Q

the only AA that is not chiral

A

glycine

no optical activity under plane-polarized light

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4
Q

4 types of AA

A
  1. hydrophobic amino acids - nonpolar side chains (alkyl groups, aromatic groups)
  2. hydrophilic (neutral) - polar side chains (hydroxyl (-OH) and sulfhydryl (-SH))
  3. hydrophilic (acidic) - amino acids that have side chains that contain carboxylic acid (COOH)
  4. hydrophilic (basic) - amino acids that have amine (-NH2)

see chart

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5
Q

pKa refers to

A

the point when two species will be in equal concentration

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6
Q

isoelectric point (pI)

A

the point between the two pKa values

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7
Q

zwitterion

A

an amino acid that has a net zero charge

  • NH3+
  • COO-
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8
Q

reverse transcription

A

generating cDNA from an RNA template (used by viruses to transcribe their RNA genomes into DNA, then integrate into the host DNA genome)

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9
Q

peptide bond

A

rigid; but can rotate, allowing proteins to fold into different shapes

the NH2 attacks the carbon of the carboxylic group. the -OH group leaves, along with one of the hydrogens from the NH2 group, forming water

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10
Q

rotation around a double bond

A

restricted due to planar geometry

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11
Q

4 levels of protein structure

A

primary (alphabet)
secondary (words)
tertiary (sentences)
quaternary

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12
Q

epigenetics

A

DNA methylation
histone modification
differentiation in type of DNA in different parts of the body

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13
Q

proteins stabilized by

A

hydrogen bonds between amino acids

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14
Q

primary structure

A

covalent bonds (amide/peptide bond)

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15
Q

secondary structure

A

hydrogen bonds

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16
Q

tertiary structure

A

ionic bonds, disulfide bonds, hydrophobic interactions, hydrogen bonding

17
Q

quaternary structure

A

(same as tertiary)

ionic bonds, disulfide bonds, hydrophobic interactions, hydrogen bonds

18
Q

C- and N-terminal*

A

n/a

19
Q

hydrolysis of protein requires…

A

proteolytic enzymes (protease), strong acids

20
Q

a method of cleaving peptide bonds

A

acid hydrolysis with heat

21
Q

proline*

A

the side chain is linked to the amino group

22
Q

amino group

A

-NH2

23
Q

alpha helix breakers

A

proline and glycine

24
Q

thiol group protein

A

cysteine

forms disulfide bridges with other cysteine

(“the cysteine chapel is filled with disulfide bridges”)

25
Q

proteolysis

A

specific cleavage of the peptide bond with the help of protease

ex. trypsin (cuts Arg and Lys), produced by the pancreas to digest food