polypeptides Flashcards

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
Q

quaternary protein structure:

protein consisting of ?

A

more than one amino acid chain

26
Q

refers to any disruption in the secondary, tertiary and quaternary levels of protein structure.

A

denaturation

27
Q

in what protein structure does denaturation not occur?

A

primary protein structure

28
Q

denaturation does not cleave the peptide bonds, therefore the ??? of structure is not altered.

A

primary level

29
Q

The physical signs of protein denaturation are ??? and ???

A

precipitation and coagulation;

30
Q

the most significant consequence of denaturation is ???

A

the loss of biological activity.

31
Q

happens in many cases when denatured protein goes back to its native biologically active form.

A

Renaturation

32
Q

Heat and UV radiation

this breaks the ??? bonds causing the folded structures of protein to ???

A

H-bonds;
uncoil or unwind into random loops

33
Q

agent of denaturation:

form intermolecular H- bonds
with the protein

A

Organic solvents

34
Q

agent of denaturation:

??? and ??? break salt linkages by altering the pH causing a change in the ionization pf ??? and ??? groups

A

Acids and bases;

-COOH and -NH2 groups.

35
Q

agent of denaturation:

Prolonged contact with ??? and ??? will also cleave peptide bonds

A

acids and bases

36
Q

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)

A

Heavy metals;
carboxylate ions;

-SH

37
Q

agent of denaturation:

??? precipitate proteins by combining with ??? and disrupting ??? (ex. Use of tannic acid for tanningleather; picric acid and tea for treating burns)

A

Alkaloid reagents;
positively charged groups;
salt linkages

38
Q

alkaloid reagents examples

A

picric acid and tannic acid