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AP Bio Unit 1: Chemistry of Life Cheat Sheet (DRAFT) by

Biochemistry and Elements of Life

This is a draft cheat sheet. It is a work in progress and is not finished yet.

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Properties of Water

Hydrogen Bonds (Polarity)
Cohesion: attracted to each other; Adhesion: attracted to other things; Surface tension: water molecule collect tighter on surface; Capillary Action: cohesion + adhesion
High Specific Heat
Resists temp change; High Hvap; Evapor­ative cooling: high nrg particles evaporate
Universal Solvent
Hydrop­hilic, repels hydrop­hobic or non-polar
 

Elements of Life

Carbon
Used to build biological molecules such as carboh­ydr­ates, proteins, lipids, and nucleic acids; used in storage compounds and cell formation in all organisms
Nitrogen
Used to build proteins and nucleic acids
Phosphorus
Used to build nucleic acids and certain lipids

DNA/RNA

DNA
Structure: antipa­rallel double helix, each strand runs opposite 5’ to 3’ orient­ation (5' phosphate and 3' hydroxyl)
-A + T takes 2 H-Bonds
-C + G takes 3 H-Bonds
-Deoxy­ribose, uses thymine, double stranded, antipa­rallel

RNA
-Ribose, single stranded, uses uracil

Both:
-Sugar, phosphate group, and a nitrog­enous base
-5’ and 3’ ends
-Nitro­genous bases perpen­dicular to sugar-­pho­sphate backbone
 

Biomol­ecules

Carbs
Sugar monomers, connected w/ covalent bonds -Struc­tures determine the properties and functions of the molecules; Nrg storage, structure and protection
Lipids
Saturated: no bends, stack, solid; Unsatu­rated: bendy, liquid; more than one double bond= polyun­sat­urated; Hydrop­hobic, hormones, store nrg and coat body (waxes­/oils)
Nucleic Acids
A five-c­arbon sugar (deoxy­ribose or ribose), a phosphate, and a nitrogen base (adenine, thymine, guanine, cytosine, or uracil); Form RNA and DNA; Held together by phosph­odi­ester H-bonds; protein synthesis
Protein
Primary structure: sequence of consti­tuent amino acids; Secondary structure: folding of the amino acid chain into alpha-­helices and beta-s­heets; Tertiary Structure: overall three-­dim­ens­ional shape of the protein and often minimizes free energy (hydro­phobic intera­ctions, disulfide bridges, H-bonds, ionic bonds); Quater­nary: arrang­ement of polype­ptide subunit