Amino Acids Flashcards

1
Q

amino acids

A

building blocks of proteins, there are 20 coded for by our DNA

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2
Q

primary sequence

A

the unique sequence of a.a.’s in each protein predicts its conformation and the properties of side chains on each amino acid dictates the associations b/w them leading to the conformation of the protein

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3
Q

general a.a. structure

A

all of the 20 a.a.’s have a common structure: the carbon is substituted w/ an amino group, a carboxylic acid group, a hydrogen, and an individual side chain (R)

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4
Q

what do side chains determine?

A

how a protein can interact w/ other molecules

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5
Q

zwitterions

A

amino acids exist in this form at physiologic pH and the amino and carboxylic groups are charged; depending on the pKa of each side chain, the group may be charged/uncharged at physiological pH

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6
Q

protonation

A

occurs at very low pH

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7
Q

deprotonation

A

occurs at very high pH

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8
Q

peptide bond

A

chemical bond that forms between the carboxyl group of one amino acid and the amino group of another amino acid (condensation reaction), and the C’s and N’s of the a.a.’s form the polypeptide backbone

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9
Q

amino acid side chain classifications

A

non-polar aliphatic, aromatic, polar uncharged, sulfur-containing and charged

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10
Q

non-polar aliphatic amino acids properties

A

hydrophobic, electrons shared and no charges to interact w/ polar molecules

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11
Q

what are the non-polar alipathic a.a.’s?

A

glycine, alanine, proline, valine, leucine, isoleucine

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12
Q

aromatic amino acids properties

A

similar ring structures but each have diff. polarity

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13
Q

what are the aromatic a.a’s?

A

phenylalaline (non-polar, hydrophobic), tryptophan and tyrosine (more polar; contain N and O)

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14
Q

uncharged polar amino acids properties

A

contain electronegative O and N atoms and therefore polar, but side groups are not charged (allows them to interact w/ polar water molecules, increasing hydrophilicity)

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15
Q

what are the uncharged polar amino acids?

A

asparagine, glutamine, serine, threonine

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16
Q

disulphide bonds

A

sulfhydryl groups of 2 cysteines oxidize to form cystine; disulphide bonds are an important conformational stabilizer and often holds diff. parts of a protein molecule or 2+ chains that make up a protein molecule

17
Q

charged amino acids properties

A

carry either a negative (acidic) charge or a positive (basic) charge

18
Q

what are the charged a.a.’s?

A

aspartate, glutamate (negatively charged); arginine, lysine and histidine (+ve charge)

19
Q

side-chain interactions

A

side-chain interactions

the charged groups on a.a.’s can interact with each other and this is considered an electrostatic interaction/bond

20
Q

sickle cell anemia

A

improper protein conformation causes RBC to be sickle shaped; genetically inherited

21
Q

homologs

A

similar proteins that have arisen from a common ancestor, often by gene duplication (mutations at the variant residue are more likely to cause problems)

22
Q

polymorphisms

A

DNA variants that occur within a specific population at a frequency greater than 1%

23
Q

posttranslational modification

A

the covalent and generally enzymatic modification of proteins during or after protein synthesis

24
Q

blood coagulation

A

coagulation enzymes and substrates must assemble on a -ve surface (e.g. platelet membrane); calcium required to bridge b/w the gamma-carboxylated proteins and the membrane surface; Vitamin K is required for γ-carboxylation and this is where the drug warfarin interferes to prevent clots

25
Q

what are the sulfur containing amino acids?

A

methionine and cysteine