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34 Cards in this Set

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Hydroxyl group
Single bond to OH

Polar, can form H-bonds
Carbonyl
O double bond to C

Polar, can form H-bonds
Carboxyl
C double to O, single to OH

Weak acid (H+ donor)
Amino
N single to two N

Weak base (H+ accepor) NH3+
Sulfhydryl
S single to H

Stabilized protien structure
Phosphate
P with 3 single O, 1 double O

Involed in energy transfer, components of DNA
Methyl
C with 3 single H

Nonpolar, found in fats
Carbohydrates
(CH2O)n n= # of carbons

Glucose = energy

Starch/glycogen = energy storage

Chitin/cellulose = structural material
Aldoses
Glucose and galactose

universal fuel & milk sugar

(have are stereo-isomers)
Ketoses
Frutose

fruit sugar

(is sturctual isomer with glucose)
5-carbon sugar
Ribose and deoxyribose

OH on 2' H on 2'
Disaccharides
Formed through dehydration synthesis

Glycosidic Bond
Polysaccharides
Many sugars together

storage in plants and animals

check more in book
Lipids
Fats, phospholipids, steroids

nonpolar, hydrophobic
Components of Fats/oils
Glycerol & 3 fatty acids

Fatty acids= carboxylic acid head + hydrocarbon tail

dehydration reaction = fat+3H2O
Saturated Fats
Solid at room temp.

C on have 2 single bonds to H, can pack close together to make a solid
Unsaturated Fats
Liquid at room temp.

Some C have double bond to another C, these create kinks in the chains which make gaps so molecules cannot pack close together.
Phospholipids
Major component of Cell Membranes.

Make of Glycerol and 2 Fatty acids and a phosphate.
Phospholipid Structure
Polar Hydrophilic head +
Nonpolar Hydrophobic tails.
Amphilpathic
contains both hydrophobic and hydrophilic regions.
Steroid
Cholesterol, Testosterone, Estrogen.

Vitamins, Precursors (cholesterol), and Hormones.
Sex Hormones
Estradiol- has HO bond and lacks Methyl group compaired to testosterone.
Amino Acids
Building blocks of Proteins

Proline, Methionine, Cysteine
Proline
AA

Unique ring structure
Methionine
AA

Nearly all proteins start with with AA
Cysteine
AA

Stabilizes protein structure.
Proteins
AA + AA = Water out + peptide chain

(Carboxyl and amino groups)
Polypeptide Chain
Always runs from Amino- terminus (N) to Carboxyl-terminus (C)
Primary (1) Structure
linear order of AA

from H3N+ to COO-
Secondary (2) Structure
Localized bending/pleating of the polypeptide chains.

Involves H Bonding of polypeptide backbone.

(see notes)
Tertiary (3) Structure
Overall 3-D shape of the protien.

Involves interaction between AA side chains.
Hydrogen bonds, Ionic bonds, Disulfide bridge, hydrophobic exclusion.
Quaternary (4) Sturcture
The fitting together of polypeptide chains (subunits) to form the final 3-D stucture of the protein.
Nucleic Acids
Storage and transmission of genetic infromation.

DNA & RNA
Nitrogenous Bases
Purines: Adenine+Guanine
Double ring structure

Pyrimidines: Cytosine, Thymine, Uracil.
Single ring Structure