7_27 Lecture 1 Proteins 1.txt
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- 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
What is a "salt bridge"? What does it do?
- 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.
What is the ionic energy equation?
- k= constant
- q1 and q2 = charged particle strength
- D= Dialectric constant (characteristic of the medium)
- r= distance
What atoms hydrogen bond? Why?
- N,O, or F.
- Due to high polarity of X-H bond.
What is the Hydrophobic effect? How does it work?
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.
What is Van der Waals Force?
Between uncharged but POLARIZABLE groups.
Evdw = -A/r^6 +B/r^12 ???????do i have to know this?
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