Protein Synthesis Flashcards
What is a protein
chain/ polymer of acid linked by peptide bond
aka polypeptide -
always drawn n (amino group) to c (carboxyl group)
What causes a peptide bond
condensation reaction/ dehydration synthesis
- coplanar/ ridged can not be rotated
What are peptide bond properties
R amino side chain can have 2 orientations
can wither be cis or trans orientation
Describe a cis orientation
less stable due to steris repulsion of side chain
Very rare
Describe trans orientation
Most common orientation with sidechains alternating
How is primary structure derived
Completely off DNA
What are the 2 type of common secondary proteins
Alpha sheet
B pleaded sheet
Describe the structure of Secondary Protein
derived from the folding cause by H bonds with the polypeptide backbone
Describe B pleaded sheets
can be parallel or anti paraelle
H bonding with backbone amine and backdone carbonyl group
alpha sheets
H bonding with backbone amine and backdone carbonyl group
tightly packed can have side chains protruding from helix
Tertiary Proteins
driven by side chains and interaction between them
Bonding can be ionic or covalent eg: hydrogen bonding, dipole-diploe/ Ionic
Quaternary structure
some proteins can be comprised of more than one polypeptide chain
multiple folded protein subunits
Structures of Globular protein
Enzymes, hemoglobin, antibodies
Structures of Fibrous structures
keratin, actin collagen, silk
Describe Globular proteins
lower stability
transport, immune, enzyme
