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Mammalian Physiology requires a basic understanding of cell biology and biochemistry. This has
been covered in previous (introductory) courses and is considered prerequisite knowledge. This
reading guide can be used to review this material using our textbook. There will be a quiz
posted on blackboard in the first week of class (week 1 quiz ) covering this material.
2-4 BIOCHEMISTRY
The study of the functioning of the human body requires basic knowledge of chemistry and
physics. Molecular interactions are essential to understand the principle of homeostasis and
other physiological principles and mechanisms. Most of the material listed below is
introductory chemistry and biology, with a focus on understanding protein function and
biological membranes.
LEARNING OBJECTIVES
29-48 Basic chemistry (a lot of it is covered in fig. 2.1- 2.6, 2.8, 2.9)
Recognize the basic structure of biochemical molecules (fig. 2.1-2.4), define:
Organic molecules, lipoproteins, glycoproteins, glycolipids
Polymers (p. 29)
Functional groups (e.g. phosphate group)
Lipids
Fatty acids – saturated vs. unsaturated fatty acids (pay attention to the double bonds)
Carbohydrates
Proteins (peptide bonds, amino acids, etc.)
Nucleotides (nucleid acid, nitrogenous bases, etc.)
Covalent and noncovalent bonds and interaction (fig. 2.5, 2.6, 2.8), define:
Cations vs anions
Polar vs nonpolar
Covalent bonds
Noncovalent bonds:
o Ionic bonds
o hydrogen bonds
o van der Waals forces
Hydrophilic vs hydrophobic interactions (or lipophobic vs. lipophilic). See also fig. 2.8
o Pay special attention to phospholipids
pH (recognize that low pH corresponds to high [H+] in a solution, see fig. 2.9)
Law of mass action: be able to predict the direction of a chemical reaction when the
equilibrium is disturbed (p. 47, 48, fig. 2.11); concept check 13
1
Week 1: Biochemistry, proteins, and membrane dynamics
List and define seven protein categories, most important ones: enzyme, signal
molecules, receptors)
Define binding/active site, substrate, ligand
Define affinity, specificity, competition, agonist, competitive antagonist (called inhibitor
in our text) (p. 46-49)
o Recognize that changes in amino acid sequence can alter protein chemistry,
affinity, specificity, etc. (it’s good to know the basic structure of amino acids and
that amino acids vary in the R group)
Activation and modulation, define allosteric modulation vs. covalent modulation and an
example of each; recognize that physical factors, such as pH can alter protein structure,
chemistry and function (p. 51)
Define saturation (p. 51)
110-118 Central dogma DNA -> RNA -> amino acid chain
Distinguish between transcription and translation (fig. 4.18)
Recognize that proteins can be modified (posttranslational modification, p. 116)
5 MEMBRANE DYNAMICS
Membrane dynamics are important for maintaining the dynamic steady states of the body’s
intracellular and extracellular compartments. Concentration differences drive the movement of
substances, which is often selective depending on the type of membrane proteins expressed
on/in a cell.
LEARNING OBJECTIVES
2
Week 1: Biochemistry, proteins, and membrane dynamics
o Recognize that molecules diffuse down the concentration gradient (p. 132-133).
o Describe the factors that determine the rate of diffusion (fig. 5.7).
Describe facilitated diffusion (p. 136)
Describe active transport and contrast it to facilitated diffusion (p. 136)
o Distinguish between primary active transport and secondary active transport (p.
142)