BIOL 112 Lecture Notes - Lecture 16: Disulfide, Carboxylic Acid, Aldehyde
16 May 2018
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Department
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BIOL 112- Lecture 2: Proteins and Nucleic Acids
Carbons can bond in a linear molecule or in a ring
C8H18 (octane)- found in plants
C6H12O6 (glucose)- found in humans
C-H bond is a nonpolar covalent bond
Functional groups:
Functional
group
Formula
Family of
molecules
Properties
Example
Hydroxyl
OH-
Alcohols
Highly polar, very
soluble, weak acid
(drop a proton)
Ethanol (C2H5O)
Phosphate
PO4-
Organic
phosphates
Breaking O-P bonds
releases a lot of energy
3-phosphoglyceric
acid (C3H5PO7)
Sulfhydryl
SH-
Thiols
In proteins, can forma
disulfide bond (S-S)
which contributes to
protein structure
Cysteine (C3H7NO2S)
Amino
NH2
Amines
Acts as a base, attracts
a proton (NH3+)
Glycine (C2H5NO2)
Carbonyl
COH-
CO-
Aldehydes
Ketones
Aldehydes react with
compounds to produce
larger molecules with
form COH2 and 2 R
groups (1 from
aldehyde and 1 from
the other reactant
Acetaldehyde (C2H4O)
Acetone (C3H6O)
Carboxyl
COOH-
Carboxylic
acids
Acts as an acid, tends
to lose a proton (COO-
with one R group)
Acetic acid (C2H4O2)
➢ Carbonyl: sugars
➢ Carboxyl: a.a, fatty acids
➢ Amino: protein
➢ R-groups: remainder, must contain a C. They determine the identity of an a.a.
Macromolecules:
- Can form huge polymers
- Proteins, nucleic acids, carbohydrates, lipids (sometimes)
- Made the same in all living things with same proportions
- Advantage: organism acquire needed biochemical by eating other organisms
Polymerization: bonding of monomers
find more resources at oneclass.com
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1. Condensation reaction: monomer in, H2O out
Uses a covalent bond
Anabolic (requires energy)
2. Hydrolysis: H2O in, monomer out
Occurs when we eat
Catabolic (releases energy)
Chemically: breaking bonds requires energy (refers to breaking 1 covalent bond)
Biology: breaking more than one bond (entire chemical reaction) thus, releases energy
Proteins:
➢ Polymer of amino acids bonded by a peptide bond (stable covalent bond)
➢ Range in size from a few a.a. to thousands of them (titin= 33 000 a.a.)
➢ Folding is crucial to the function of a protein and is influence largely by the
sequence of a.a.
➢ Most abundant macromolecule in the body
Non-ionized form:
Ionized form:
Recognizing properties:
1. Nonpolar side chains (all C-H bonds, not
soluble in water)
2. Polar side chains (OH, CO bonds & carbonyl
R groups, soluble from partial charges)
3. Charged (COO- or a.a. side chain groups,
highly soluble)
For exam: know how to draw proteins
- alpha carbon is attached to an amino
group, carboxyl group, R-group
find more resources at oneclass.com
find more resources at oneclass.com
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BIOL 112 Full Course Notes
Verified Note
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Document Summary
Biol 112- lecture 2: proteins and nucleic acids. Carbons can bond in a linear molecule or in a ring. Highly polar, very soluble, weak acid (drop a proton) Breaking o-p bonds releases a lot of energy. In proteins, can forma disulfide bond (s-s) which contributes to protein structure. Acts as a base, attracts a proton (nh3. Aldehydes react with compounds to produce larger molecules with form coh2 and 2 r groups (1 from aldehyde and 1 from the other reactant. Acts as an acid, tends to lose a proton (coo- with one r group) R-groups: remainder, must contain a c. they determine the identity of an a. a. Made the same in all living things with same proportions. Advantage: organism acquire needed biochemical by eating other organisms. Polymerization: bonding of monomers: condensation reaction: monomer in, h2o out. Anabolic (requires energy: hydrolysis: h2o in, monomer out. Chemically: breaking bonds requires energy (refers to breaking 1 covalent bond)
