Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
14 Cards in this Set
- Front
- 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. |