Proteins CH 3.2 Flashcards
Properties of Proteins
Enzymes Defense Proteins Hormonal/Regulatory Receptor Storage Structural Transport Genetic Regulatory
Amino Acids
- Building Blocks of Proteins
- Central Carbon (alpha) attached to Nitrogen containing amino group + Carboxylic Acid group + Hydrogen + R Group
- Each AA is defined by its R Group
Cystine
Amino Acid w/ SH group
Allows for the formation of disulfide bridge between AA’s
Determines folding of AA
Glycine
Smallest AA
R-group = Hydrogen
Proline
Ring = stabalizer
AA’s are bonded together by…
Peptide linkage
Direction of polymerization
Amino to Carboxyl direction (N terminus to C terminus)
The covalent bond that holds AA together = peptide bond
Primary Structure
Polymerization of AA’s
Line of AA’s held together by peptide bonds
Secondary Structure
Hydrogen bonding (H-bonding)
Alpha Helix
Beta-pleated sheets
Alpha Helix
Secondary Structure
Right Handed coil shape
N-H and C=O Hydrogen Bond together
Beta-pleated Sheet
Secondary Structure
2 or more polypeptide chains involved
Tertiary Structure
3D Shape Bent at specific sites R-groups and AA side chains involved Disulfide Bridges --> cysteine Hydrogen bonds --> stabalize Hydrophobic side chains --> interior of protein (away from H2O) van der Waals interactions --> stabalize Ionic--> Salt Bridges
Secondary and Tertiary Structure derive from….
Primary Structure
Shape determines function–> primary structure determines sequence of AA which then determine shape and function
Quatrenary Structure
Subunits bind together
Hydrophobic interactions
H-bonds
Ionic Interactions
How are Proteins Denatured?
High Temp
Change in H+ concentrations (acidity)
High Concentrations of polar solvents
