CH 301, BMB I

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CH 301, BMB I

• Dr. Ruth Reed
• Fall semester, 2004

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Berg, Tymoczko, Stryer, Ch 1 1.1-1.2 Ask if
any questions 1.3 Chemical bonds in
biochemisty Covalent polar, nonpolar
energies in range of 100 kcal/mol or 400 kJ/mol
chemical reactionbreaking and
reforming covalent
bonds arrow pushing Example
ammonia addition to formaldehyde (p 9)
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1.3 Chemical bonds in biochemisty (contd)
Noncovalent electrostatic
(1 kcal/mol, 4 k/J/mol) hydrogen bonds (1-3
kcal/mol, 4-13 kJ/mol) van der Waals
interactions (1 kcal/mol, 4 kJ/mol
(max)) Water hydrogen bonding
dielectric constant 80. Water
diminishes the strength of electrostatic
attractions by a factor of 80 compared with the
strength of those same interactions in a vacuum.
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Ch 1, contd Thermodynamics 1. Total energy
is constant 2. Entropy of system
surroundings increases (Entropy
disorder,
randomness, probability) Biological systems
Temperature is constant (even cold-blooded
animals, plants, etc.) Constant
temperature DG DH TDS DG free energy
(negative spontaneous) DH enthalpy
(heat) TDS T times entropy (probability)
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Ch 1.3.4 Protein folding Can be rationalized
based on thermodynamics The folding process
can occur when the combination of the entropy
associated with the hydrophobic effect and the
enthalpy change associated with hydrogen bonds
and van der Waals interactions make the overall
free energy negative.
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Ch 2 Biochemical Evolution Teleology the use
of ultimate purpose or design as a means of
explaining natural phenomena Page 38summary
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Amino acids building blocks for proteins
Memorize Names, 3-letter code, 1-letter
code, pKa values
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