Peptides and Proteins Flashcards
Amphoteric
Can accept a proton ( decrease pH (acidic) so pH < pKa)
Can donate a proton (Increase pH (basic) so pH > pKa)
Isoeletric point
pKa1 + pKa2
_____________ = pI
2
pKa of Carboxilic acid group (in acidic conditions)
~ 2
pKa of Amino group (in basic conditions)
~ 9-10
Oligopeptide
2-20 amino acid residues
Polypeptide
20+ amino acid residues
Peptide bond
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
Primary structure
Covalent Peptides; Linear sequence of amino acids
Secondary Structure
Hydrogen Bonds; local folded structures that form within a polypeptide due to interactions between atoms of the backbone (alpha helix and beta sheets)
Tertiary Structure
Hydrophillic / Hydrophobic bonds; 3D structure of the polypeptide (Salt bridges and disulfide bridges)
Quaternary Structure
Interactions between 2+ polypeptide chains (molecules coming together)
Conjugated Proteins
Amino acids + Other molecule such as organic molecules
Ex: Lipoprotein (lipids); Glycoprotein (cabohydrates) ; Nucleoprotein (nucleic acids)
Denaturation
Disruption of tertiary structures of protein (causes loss of 3D structure / shape)
Temp. Denaturation
Increase the kinetic energy of molecules overcoming the hydrophobic interactions, making the protein unfold
Solute Denaturation
Interfere with secondary, tertiary and quaternary structures by disrupting hydrogen bods and disulfide bridges