Protein chemistry lecture 2 Flashcards
Peptide bond
This is formed through a reaction with an amide group and carbonyl group resulting in a 50% double bond character bond. The molecule formed mainly exists in a planar cis conformation.
Hydrolysis of peptide bonds
Can be hydrolyzed in a very slow manner unless in the presence of an enzyme. Amide bonds can spontaneously hydrolyze break off and disperse into ammonia in many situations (what are these situations?).
Isopeptide bond formation
Glutamine/lysine and asparagine when in contact with one another form peptide bonds to one another creating an isopeptide bond and an ammonia side group.
Reactions of sulfhydral groups
- Acid base reaction: A cystiene group is deprotonated resulting in the production of thiolate anion a highly reactive nucelophile
- Disulfide bond formation-sulfide molecules bond together when adjacent in space (even if far apart in seq.) and a disulfide bond is formed stabalizing the molecule.
- Reacts with oxygen to produce a so2 group compound which dissociates and becomes a charged molecule
Dehydroalanine reactions
OH group comes in and deprotonates an H group leading to the break of a sulfhydral group a formation of a double bond between two carbon atoms making it highly reactive. Lysine, cystiene and or amino groups can add across it and crosslink with it.
Mailard browning reactions
carbonyl reacts with amino group to form a shiff base which undergoes multiple rearrangments producing various flavor compounds
Protein polymers
long sequence of amino acids which are the same if encoded by the same gene
Polypeptide chain and entropy
Protein chains are very flexible and can fold into a variety of conformations but in order to fold, the protein chain requires energy to overcome entropy which causes it to be in an unfolded state.
Beta and alpha structure
Alpha-Right handed helical, side chains stick out and are bonded together by H bonds.
Beta sheets- two types, parallel and antiparralel stabalized by h bonds
dihedral angles
3 bonds arranged in angles that provide for the specific orientation of amino acids in space