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14 Cards in this Set

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  • Back

What is an amino acid?

Organic molecule containing an amine, carboxylic acid, hydrogen, and unique side chain around a central carbon

What is a peptide?




What is a main-chain/backbone?




What is a side-chain?

Peptide = A series of amino acids joined by peptide bonds.




Main-chain = Regularly repeating part of a polypeptide chain




Side-chain = Variable part of a polypeptide chain

Primary level of protein structure

Amino acid sequence (no structure)

Secondary level of protein structure

Local structural elements that are held together by main chain H bonds. They are typically repeating structures (alpha helix, beta sheet)

Tertiary level of protein structure

The association of secondary elemental to form a globular structure.




H bonds and hydrophobic interactions between side chains are major drivers.

Quaternary level of protein structure

The association of two or more subunits to form a complex.




Interacting surfaces must have shape and chemical complementarity.

An amino acid "residue" consists of what?

An alpha carbon with four substituents:


-Amine group


-side chain (R)


-hydrogen


-carboxylic acid

What does it mean to be chiral?

Associated with asymmetrical carbon atoms.




The carbon is bound to 4 different atoms or groups of atoms




Amino acids and proteins are chiral

Intramolecular forces

Bonding forces within molecule




-covalent bonds within a protein's primary structure (ex: peptide bond)

Intermolecular forces

Non-bonding forces between molecules




-non covalent bonds outside of a protein's primary structure (ex: H bonding between main chain backbone)

Hydrogen Bonding

The sharing of a hydrogen between two electronegative atoms.




-H bond donor = electronegative atom covalently bound to a H atom


-H bond acceptor = electronegative atom with accessible lone pair




(in biological systems, we typically are talking about O and N as the atoms involved in H bonding)

What is enalaprilat?

Used to treat high blood-pressure. It is an ACE inhibitor and antihypertensive.




Enalaprilat forms weak, non covalent interactions with ACE that provide affinity (strength of the interaction) and specificity (the exclusivity of the interaction)



Ionic Interactions

Proteins can interact with charged groups via ionic interactions. Three types of ionic interactions are:


-Ion-ion (salt bridge)


-Ion-dipole


-Ion-induced dipole

Hydrophobic Interactions

Non polar groups can contribute binding energy and specificity.




Non polar and polar groups spontaneously separate like oil and water.




Clustering allows the surrounding water to be less structured and entropy increases.