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Biochemistry

CHEM 271
Brandon Findlay
S P 2 6 5 . 2 2 O ff i c e H o u r s Tu e 1 0 : 3 0 1 2 : 0 0 ,
T h u r. 3 : 0 0 5 : 0 0
B r a n d o n . F i n d l a y@ C o n c o r d i a . c a

Class Outline
GRADING
Tutorials and labs

25%

Online quizzes

5%

Midterms

35% (15+20 or 20+15)

Final

35%

Class notes are posted 24 hr in advance (moodle).

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Assignments are unlocked three days before each class.


Due one week after.

Sapling is recommended, but not required.


If you dont enroll the 5% will be folded into your final (for a
weighting of 40%).

The Academic Code of Conduct:


Ethical Use of Information Sources
(CHEM 101)
Required (letter grade/incomplete penalty)

You are exempt if you took the course on/after Fall 2010. Otherwise, sign up outside
the Chem/Biochem office.

Biochemistry?

Biochemistry

Biology

Chemistry

The study of chemical principles in biological systems


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What will we be studying?


Part 1: Structure and properties of proteins

Tertiary (3D) structure

Quaternary
structure
- Hemoglobin
(structure & function)
- Characterizing proteins
Enzymes
(structure & function)
- Serine proteases

Secondary structure

- Amino acids (20)


- Acids/bases
- Primary structure / non-covalent
interactions

Enzyme kinetics
Enzyme inhibitors

Source: Dr. Steven Kawai6

What will we be studying?

Part 2: Central metabolism (Glucose ATP): enzymes, regulation,


strategy, thermodynamics

Citric acid cycle


Energy capture and
biosynthetic
intermediates

Carbohydrates
(structure & function)

Metabolism
- Glycolysis
- Gluconeogenesis
- Glycogen metabolism
- Cofactors

Enzyme regulation strategies

Oxidative phosphorylation
(Electron-transport chain)

Oxidative phosphorylation
(ATP synthesis)
ATP is the major storage
form of energy in the cell

Chemical Interactions, a Summary


Van der Waals
Interactions

Covalent
bonds

Hydrogen
Bonds

Electrostatic
Interactions

http://chemed.chem.purdue.edu/genchem/topicreview/bp/1biochem/4frame.html

Hydrogen Bonds are Directional


Very important for substrate binding and
protein folding.

The Hydrophobic Effect


Non-polar groups form only weak bonds.
In a polar solvent free energy is maximized by
excluding non-polar groups.

Amrit Kessel. https://amit1b.wordpress.com/computational-biophysics/

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The Elements of Life


Se
Fe Cu Mn
Other transition metals

P
S

Cl Na
Mg K Ca

CHON
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Cellular Building Blocks


Proteins
structure, catalysis, motion, signaling

Carbohydrates
Energy, storage of energy

Lipids
Energy, cell membranes

Nucleic acids
Genetic information

Small molecules
Cofactors, secondary metabolites (antibiotics, etc.)

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The Central Dogma


Transcription

DNA

Translation

RNA

Protein
[1(+) per gene]

Information as coded sequences of


chemical letters

structural building blocks


receptors
transporters
enzymes

* Chapter 1 of the textbook reviews the structure and function of


nucleic acids.

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A possible evolutionary timeline


NH4 + CH4 + H2O + H2 + electricity
(Miller-Urey experiment on abiogenesis)

>20 amino acids

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The Tree of Life: 3 Domains, 1 Ancestor

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Proteins are Conserved Through Time

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Amino Acids are the Building Blocks of Proteins


Gly

Gln

Ser

Lys

Leu

Tyr

Asp

Glu

Trp

Met

Arg
Ile

N
C

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Amino acids
20 common structures.
Secondary metabolites and bio-engineered proteins
can contain many more, including D-amino acids.

Ribosomal

Non-ribosomal

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Hydrophobic AA: Part 1

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Hydrophobic AA: Part 2

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Polar AA: Part 1

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Polar AA: Part 2

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Negatively Charged Amino Acids

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Positively Charged Amino Acids

pKa!!!

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Histidine, a special case

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Know the Abbreviations!

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What to Know
Types of chemical interactions.
Characteristics of the 20 common amino acids.
Structure.
Abbreviations (3 letter and 1 letter).

Physical properties (polar, hydrophobic, etc.)

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