3D Structure of Proteins Flashcards
4 Interactions in Proteins
- Hydrophobic Effect
- Hydrogen Bonds: lead to alpha helix and beta sheet structures
- London Dispersion: Weak interactions between atoms contributes to stability of interior of the protein
- Electrostatic Interactions: Strong interactions
What are the repeating atoms in the peptide backbone
N-C-C
Characteristics of the peptide bond
- Planar
- Polar
- Rigid
- Limited rotation around peptide bond
- Behaves like a double bond
what bond is the peptide bond (atom wise)
C-N bond
Why is rotation around the peptide bond not permitted
Due to the resonance structure
Rotations around what bonds are permitted
Rotations around bonds connected to the alpha carbon are permitted:
* The alpha carbon - carbon bond (carbonyl carbon bond)
* The alpha carbon - nitrogen bond (amide nitrogen bond)
What does secondary structure refer to
- Local spatial arrangement
- Interactions within the polypeptide backbone
What are both alpha helices and beta sheets stabilised by
hydrogen bonds
What is irregular arrangement of the polypeptide chain called
Random coil
Which AAs are strong helix formers
Alanine (Ala)
Leucine (Leu)
What AAs are helix breakers and why (2)
- Proline (Pro): the rotation around the alpha carbon - nitrogen bond is impossible
- Glycine (Gly): the tiny R group supports other conformations (R group = H)
What creates a pleated sheet like structure
- The planarity of the peptide bond
- The tetrahedral geometry of the alpha carbon
What are beta sheets held together by
The hydrogen bonding of amide and carbonyl groups of the peptide bond from opposite strands
Characteristic of the h. bonds in parallel beta sheets
The hydrogen bonds between strands are bent and therefore weaker
Characteristic of the h. bonds in antiparallel beta sheets
The h. bonds between sheets are linear (straight) and therefore stronger