Bio 21 Cell Biology

List of Terms and Study Guide

For MiniExam 1, 12 February 2001

 

eukaryotic

prokaryotic

endosymbiotic

membrane-bound compartments

organelle

plasma membrane

nucleus

nuclear envelope

cytoplasm

mitochondria

chloroplasts

plastids

genome

peroxisomes

ER (endoplasmic reticulum)

ribosomes

Golgi

lysosomes

phagosome

cytosol

cytoskeleton

 

neutrons

protons

electrons

covalent bond

polar covalent

ionic bonds

H bonds

mole

molecular weight

common elements of living organisms

CHNO

carbon bonds

methyl group

amino group

carboxyl group (carboxylic acid)

alcohol

pH

acid

base

amino acid

alpha C

R group (side chain)

nonpolar

basic

acidic

uncharged polar

peptide bond

condensation reaction (dehydration synthesis)

peptide

polypeptide

protein

subunit

monomeric

multimeric

primary sequence

N-terminus

C-terminus

20n

secondary sequence

alpha helix

ß-pleated sheet

parallel

antiparallel

hydrophilic

hydrophobic

amphipathic

tertiary structure

quartnerary structure

monomer

homodimer

heterodimer

trimer

tetramer

molecular chaperone/heat shock protein

noncovalent bonds

hydrophobic interactions

disulfide bonds

extracellular

cytosolic

denature

oxidized

reduced

renature

random coil

stable conformation

unstable intermediate

 

antibody (Ab)

heavy chain

light chain

variable loop/region

antigen binding

ligand

affinity

thermally induced motion

equilibrium

association vs dissociation

 

PANELS TO FOCUS ON
1-2
2-1, 2-2, 2-5, 2-7

FIGURES TO FOCUS ON
1-12, 1-14, 1-17
2-2, 2-6, 2-13, 2-20, 2-22, 2-26, 2-28

1. Know how eukaryotes differ from prokaryotes (e.g. presence of membrane-bound organelles). Know the arguments supporting the endosymbiotic origin of eukaryotic cells.

2. Be able to recognize the various components that make up a eukaryotic cell. Have a general understanding of the function of each (e.g. mitochondria generate ATP through food oxidation; plastids such as chloroplasts generate ATP through photosynthesis).

3. Be able to draw a generic amino acid and label the subgroups (R group, amino group, carboxyl group). Be able to draw an a.a. in both its ionized and unionized forms.

4. Be able to recognize the various classes of amino acids: basic, acidic (in both ionized and unionized form), nonpolar, and uncharged polar.

5. Be able to recognize interactions between amino acids that form H bonds, ionic bonds, or result in hydrophobic interactions.

6. Know the types of interactions (chemical bonds) that stabilize primary, secondary, tertiary, and quaternary levels of protein structure.

7. Be able to show how a peptide bond is formed through a dehydration synthesis (condensation reaction).

8. Be able to show how serine, threonine, and tyrosine can be targets of phosphorylation.

9. Understand the difference between a base and an acid, how they function in water,how such interactions affect the behavior of individual amino acids, and how multiple such interactions contribute to the stucture and behavior of a polypeptide or protein.

10. Know the polar (or nonpolar) nature of covalent bonds between the most common elements in living organisms (i.e., C-H, N-H, O-H).

11. Know which amino acids are capable of forming disulfide bonds (i.e., cysteine), under what conditions they will form (i.e., oxidative rather than reducing environment), and what levels of protein structure they can help stabilize (tertiary and quaternary).

12. Know the sequence of atoms and the nature of their bonds that make up the polypeptide backbone.

13. Know how to recognize the amino or N-terminus vs the carboxy or C-terminus of a polypeptide.

14. Know how to identify an alpha helix and ß pleated sheet (sometimes referred to as simply a ß sheet). Know how these structures are stabilized by H-bonds. Know the difference between a parallel and antiparallel ß sheet. Know how the amino acid side chains (the R groups) are arranged in space in both an alpha helix and ß sheet. Understand how the class of amino acids (i.e., nonpolar, polar, or charged) forming an alpha helix or ß sheet can make the structure hydrophilic, hydrophobic, or amphipathic.