Peptides and Proteins Flashcards

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1
Q

Amphoteric

A

Can accept a proton ( decrease pH (acidic) so pH < pKa)

Can donate a proton (Increase pH (basic) so pH > pKa)

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2
Q

Isoeletric point

A

pKa1 + pKa2
_____________ = pI
2

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3
Q

pKa of Carboxilic acid group (in acidic conditions)

A

~ 2

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4
Q

pKa of Amino group (in basic conditions)

A

~ 9-10

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5
Q

Oligopeptide

A

2-20 amino acid residues

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6
Q

Polypeptide

A

20+ amino acid residues

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7
Q

Peptide bond

A

Functional group -C(O)NH - formed when an nucleophillic amino group attacks an electrophilic carbonyl through a condensation (dehydration) reaction

**Reverse = Hydrolysis rxn to break a peptide bond

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8
Q

Primary structure

A

Covalent Peptides; Linear sequence of amino acids

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9
Q

Secondary Structure

A

Hydrogen Bonds; local folded structures that form within a polypeptide due to interactions between atoms of the backbone (alpha helix and beta sheets)

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10
Q

Tertiary Structure

A

Hydrophillic / Hydrophobic bonds; 3D structure of the polypeptide (Salt bridges and disulfide bridges)

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11
Q

Quaternary Structure

A

Interactions between 2+ polypeptide chains (molecules coming together)

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12
Q

Conjugated Proteins

A

Amino acids + Other molecule such as organic molecules

Ex: Lipoprotein (lipids); Glycoprotein (cabohydrates) ; Nucleoprotein (nucleic acids)

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13
Q

Denaturation

A

Disruption of tertiary structures of protein (causes loss of 3D structure / shape)

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14
Q

Temp. Denaturation

A

Increase the kinetic energy of molecules overcoming the hydrophobic interactions, making the protein unfold

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15
Q

Solute Denaturation

A

Interfere with secondary, tertiary and quaternary structures by disrupting hydrogen bods and disulfide bridges

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16
Q

Detergent Denaturation

A

Can solubilize proteins

17
Q

Amino Acid Placement in Proteins

A

Hydrophobic amino acids tend to reside inside proteins

Hydrophillic amino acids tend to reside on the outside of proteins