polypeptides Flashcards

(38 cards)

1
Q

is amide linkage formed by the reaction between α-carboxyl group of one amino acid and α-amino group of another amino acid with the elimination of water molecule

A

Peptide (peptide bond)

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2
Q

two amino acids are combined

A

Dipeptide

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3
Q

3 to 10 amino acids combined

A

Oligopeptide

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4
Q

> 10 amino acids combined

A

Polypeptide

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5
Q

300-1000 amino acids combined

A

Proteins

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6
Q

There are four levels of protein structure:

A

primary
secondary
tertiary
quarternary

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7
Q

linear sequence of amino acids

A

primary

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8
Q

regular patterns formed by primary structure folding

A

secondary

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9
Q

completely folded polypeptide with one or more domains

A

tertiary

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10
Q

association of multiple polypeptides; not found in all proteins

A

quaternary

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11
Q

The simplest level of protein structure is simply the amino acid sequence within a polypeptide chain.

A

the primary structure

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12
Q

Understanding the ??? is important because many genetic diseases results in protein with abnormal amino acid sequences

A

primary structure of proteins

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13
Q

is local interactions between stretches of a polypeptide chain and includes α-helix and β-pleated sheets structures.

A

Secondary structure

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14
Q

is primarily due to interactions between the R groups of amino acid which make up the protein.

A

The tertiary structure

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15
Q

R group interactions (4)

A

§ hydrogen bonding
§ ionic bonding
§ dipole-dipole interactions
§ London dispersion forces

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16
Q

are also important for the tertiary structure, in which amino acids with non-polar, hydrophobic R groups cluster together within the protein, leaving hydrophilic amino acids outside to interact with surrounding water molecules.

A

Hydrophobic interactions

17
Q

One specific form of covalent bond may contribute to tertiary structure: the

A

disulfide bond

18
Q

Many proteins however consist of several polypeptide chains, also known as ???

19
Q

They give the protein its quaternary form, as these subunits come together.

20
Q

One example of a ???
is hemoglobin.

A

quaternary-structured protein

21
Q

In general, the same types of interactions that lead to tertiary structure also hold the
subunits together to give ???

A

quaternary structure

22
Q

interactions that lead to tertiary structures are mostly ???

A

weak interactions,

such as hydrogen bonding and dispersion forces in London

23
Q

??? protein structure;

??? bonding of the peptide backbone causes amino acids to fold into a ??? pattern

A

secondary;

hydrogen;

repeating

24
Q

tertiary protein structure:

3-D folding pattern of a protein due to ??? interactions

A

side chain interactions

25
quaternary protein structure: protein consisting of ?
more than one amino acid chain
26
refers to any disruption in the secondary, tertiary and quaternary levels of protein structure.
denaturation
27
in what protein structure does denaturation not occur?
primary protein structure
28
denaturation does not cleave the peptide bonds, therefore the ??? of structure is not altered.
primary level
29
The physical signs of protein denaturation are ??? and ???
precipitation and coagulation;
30
the most significant consequence of denaturation is ???
the loss of biological activity.
31
happens in many cases when denatured protein goes back to its native biologically active form.
Renaturation
32
Heat and UV radiation this breaks the ??? bonds causing the folded structures of protein to ???
H-bonds; uncoil or unwind into random loops
33
agent of denaturation: form intermolecular H- bonds with the protein
Organic solvents
34
agent of denaturation: ??? and ??? break salt linkages by altering the pH causing a change in the ionization pf ??? and ??? groups
Acids and bases; -COOH and -NH2 groups.
35
agent of denaturation: Prolonged contact with ??? and ??? will also cleave peptide bonds
acids and bases
36
agent of denaturation: ??? like Hg+2, Ag+, Pb2+ and their salts form stronger bonds with ??? of acidic amino acids. It also cleaves the ??? bonds (ex. The use of egg albumin as antidote for heavy metal poisoning)
Heavy metals; carboxylate ions; -SH
37
agent of denaturation: ??? precipitate proteins by combining with ??? and disrupting ??? (ex. Use of tannic acid for tanningleather; picric acid and tea for treating burns)
Alkaloid reagents; positively charged groups; salt linkages
38
alkaloid reagents examples
picric acid and tannic acid