7_27 Lecture 1 Proteins 1.txt

• author "Joshua Ellis"
• tags "HUCM"
• description ""
• fileName "7/27 Lecture 1 Proteins 1"
• freezingBlueDBID -1.0
• What are the four key Non-Covalent Molecular Interactions
• Ionic Interactions (salt bridge)
• Hydrogen Bonding
• The Hydrophobic effect
• Van der Waals forces

• Forms between residues of opposite charge in proteins.
• Allows charged residues to be present within proteins and helps stabilize structure.

also: further apart the weaker they are.

E=kq1q2/D(r)^2

• E=energy
• k= constant
• q1 and q2 = charged particle strength
• D= Dialectric constant (characteristic of the medium)
• r= distance

• N,O, or F.
• Due to high polarity of X-H bond.

In which groups of non polar molecules stick together when surround by polar solution. Induces order into a system, lowering entropy, and thus energy.

ex: proteins with hydrophobic cores.

Between uncharged but POLARIZABLE groups.

Evdw = -A/r^6 +B/r^12 ???????do i have to know this?