Biology 111 Exam One
Terms
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- Hydroxyl group
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Single bond to OH
Polar, can form H-bonds - Carbonyl
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O double bond to C
Polar, can form H-bonds - Carboxyl
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C double to O, single to OH
Weak acid (H+ donor) - Amino
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N single to two N
Weak base (H+ accepor) NH3+ - Sulfhydryl
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S single to H
Stabilized protien structure - Phosphate
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P with 3 single O, 1 double O
Involed in energy transfer, components of DNA - Methyl
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C with 3 single H
Nonpolar, found in fats - Carbohydrates
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(CH2O)n n= # of carbons
Glucose = energy
Starch/glycogen = energy storage
Chitin/cellulose = structural material - Aldoses
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Glucose and galactose
universal fuel & milk sugar
(have are stereo-isomers) - Ketoses
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Frutose
fruit sugar
(is sturctual isomer with glucose) - 5-carbon sugar
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Ribose and deoxyribose
OH on 2' H on 2' - Disaccharides
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Formed through dehydration synthesis
Glycosidic Bond - Polysaccharides
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Many sugars together
storage in plants and animals
check more in book - Lipids
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Fats, phospholipids, steroids
nonpolar, hydrophobic - Components of Fats/oils
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Glycerol & 3 fatty acids
Fatty acids= carboxylic acid head + hydrocarbon tail
dehydration reaction = fat+3H2O - Saturated Fats
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Solid at room temp.
C on have 2 single bonds to H, can pack close together to make a solid - Unsaturated Fats
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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
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Major component of Cell Membranes.
Make of Glycerol and 2 Fatty acids and a phosphate. - Phospholipid Structure
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Polar Hydrophilic head +
Nonpolar Hydrophobic tails. - Amphilpathic
- contains both hydrophobic and hydrophilic regions.
- Steroid
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Cholesterol, Testosterone, Estrogen.
Vitamins, Precursors (cholesterol), and Hormones. - Sex Hormones
- Estradiol- has HO bond and lacks Methyl group compaired to testosterone.
- Amino Acids
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Building blocks of Proteins
Proline, Methionine, Cysteine - Proline
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AA
Unique ring structure - Methionine
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AA
Nearly all proteins start with with AA - Cysteine
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AA
Stabilizes protein structure. - Proteins
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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
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linear order of AA
from H3N+ to COO- - Secondary (2) Structure
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Localized bending/pleating of the polypeptide chains.
Involves H Bonding of polypeptide backbone.
(see notes) - Tertiary (3) Structure
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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
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Storage and transmission of genetic infromation.
DNA & RNA - Nitrogenous Bases
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Purines: Adenine+Guanine
Double ring structure
Pyrimidines: Cytosine, Thymine, Uracil.
Single ring Structure