4. Amino Acids and Proteins Flashcards

1
Q

What is an α-amino acid?

A

an amino acid in which the amino group is attached to the carbon atom adjacent to the carboxyl group

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2
Q

What is aggregation?

A

Several things grouped together or considered as a whole

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3
Q

What is chymotrypsin?

A

a digestive enzyme thatcleaves peptide bonds of proteins where the amide side of the bond is an aromatic amino acid like tyrosine, phenylalanine or tryptophan. Used to sequence amino acids

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4
Q

What us cyanogen bromide?

A

an inorganic compound used to sequence amino acids by cleaving the C-terminus of methionine

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5
Q

What is a D-configuration?

A

a compound that when represented as a Fischer projection with the carboxyl group pointing up, has its amine group on the right

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6
Q

What is a disulfide bridge?

A

a covalent bond between two sulfur atoms, i.e. an - S - S - bond

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7
Q

What is Edman degradation?

A

a method of sequencing amino acids in a peptide. In this method, the amino-terminal residue is labeled and cleaved from the peptide without disrupting the peptide bonds between other amino acid residues

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8
Q

What is a Fischer projection?

A

two-dimensional representations that show the configuration of a stereocentre; horizontal lines represent bonds projecting forward from the stereocentre, vertical lines represent bonds projecting to the rear

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9
Q

What is gel electrophoresis?

A

a method for separation and analysis of macromolecules (DNA,RNAandproteins) and their fragments, based on their size and charge

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10
Q

What is the hydrophobic effect?

A

the observed tendency of nonpolar substances to aggregate in aqueous solution and exclude water molecules.

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11
Q

What is an isoelectric point?

A

the pH at which an amino acid, a polypeptide or protein has no net charge

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12
Q

What is an L-configuration?

A

a compound that when represented as a Fischer projection with the carboxyl group pointing up, has its amine group on the left

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13
Q

What are peptidases?

A

any enzyme that performs proteolysis; protein catabolism by hydrolysis of peptide bonds

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14
Q

What is a peptide?

A

a short polymer of amino acids

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15
Q

What is a primary structure?

A

the sequence of smaller molecular components that are assembled to make a biopolymer; thus for proteins and peptides it is the specific amino acids in a polypeptide chain read from the N-terminal amino acid to the C-terminal amino acid

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16
Q

What is a quaternary structure?

A

the arrangement of polypeptide monomers into a noncovalently bonded aggregation

17
Q

What is a secondary structure?

A

the ordered arrangement (conformation) of a biopolymer; this the organised shaped of the chain of amino acids in localised regions of a polypeptide or protein, seen as sheets or coils.

18
Q

What is a tertiary structure?

A

the three-dimensional arrangement in space of all atoms in a single polypeptide chain

19
Q

What is trypsin?

A

a chemical used to sequence amino acids by cleaving the polypeptide chain at points where a arginine or lysine are present

20
Q

What is zwitterion?

A

an ionic salt in which both cation and anion are part of the same molecule

21
Q

What determines the behaviour of the amino acid in water and how the peptide folds?

A

The nature of the amino acid r-group

22
Q

Are all amino acids chiral?

A

No - glycine is not chiral but the others are

23
Q

What do horizontal lines on a Fischer projection represent?

A

Bonds projecting forward

24
Q

What do vertical lines on a Fischer projection represent?

A

Bonds projecting to the rear

25
Q

Which configuration is most amino acids in?

A

L-configuration

26
Q

Which amino acid is the only R configuration using the R,S system?

A

Cysteine - the rest are S, except glycine which is achiral

27
Q

What does cyanogen bromide do?

A

It is a molecule specific for cleavage of peptide bonds formed by the carboxyl group of methionine

28
Q

Which amino acids does trypsin cleave?

A

Arginine and lysine

29
Q

Which amino acids does chymotrypsin cleave?

A

Phenylalanine, tryptophan and tyrosine

30
Q

What does edman degradation do?

A

Cleaves the n-terminal amino acid allowing it to be identified