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BIO 264 BIOCHEMISTRY
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Ionic Bonding
gaining electrons
losing electrons
a transfer of one or more electrons from one atom to another to fill the outer orbital
Cation
an ion with a positive charge
Anion
an ion with an negative charge
Covalent Bonding
sharing electrons
electrons are shared to fill the outer orbital
Single covalent bonds
Share 2 electrons
one pair on electrons
Double covalent bonds
Share 4 electrons
two pair of electrons
Triple covalent bonds
Share 6 electrons
three pair of electrons
Hydrogen Bonding
unequal sharing of electrons; there is a region of positive charge and a region of negative charge on the molecule
Example of Hydrogen Bonding
water
oxygen region is slightly negative since electrons are drawn closer to oxygen nucleus
hydrogen regions of water are slightly positive since electrons are closer to oxygen but the positive proton of hydrogen remains
Polar Covalent
unequal sharing of electrons
Nonpolar Covalent
equal sharing of electrons
hydrophilic
water soluble BUT insoluble in lipid
hydrophobic
insoluble in water BUT lipid soluble
acid
releases a hydrogen ion (H+) or proton
(proton donor)
base
a hydrogen ion or proton acceptor
(acceptor)
pH
measure of the hydrogen ion concentration in a solution
acid
below 7
base
above 7
neutral
7
buffers
minimize or resist pH changes
blood pH
7.4 +/-
acidosis
pH below 7.4
alkalosis
pH above 7.4
important functional groups
hydroxyl (OH)
amino (NH
2
)
carboxyl (COOH)
examples of inorganic
H
2
O
O
2
CO
2
electrolytes
organic molecules
contain carbon and hydrogen
proteins
carbohydrates
lipids
nucleic acids
vitamins + other organic molecules
Types of protein
structural protein
contractile or muscle protein
immunological or antibodies
hormones
transport or carrier proteins
enzymes
structural protein
collagen
keratin
elastin
spectrin
contractile or muscle protein
actin
myosin
immunological or antibodies
defense against disease
hormones
regulatory proteins; regulate metabolism
transport or carrier proteins
blood and cell membranes
How many "common" amino acids?
20
nonessential amino acids
body can synthesize
essential amino acids
required in diet
amino acid structure
central carbon
amion group
acid or carboxyl group
hydrogen
"R" group
structure of protein
amino acids bonded together
(dehydration synthesis)
protein
50 or more amino acids in the chain
peptide
less than 50 amino acids in chain
dehydration synthesis
smaller molecules bond together to form a larger molecule
hydrolysis
bonds between subunits of a larger molecule are broken to release the smaller subunits
denaturation
protein structure or shape is altered by changes in temperature and pH
Levels of protein structure
primary structure
secondary structure
tertiary
quaternary
primary protein structure
sequence of amino acids
secondary protein structure
helix or twisting
tertiary protein structure
folding
quaternary protein structure
several chains
hemoglobin
substrate
molecule or molecules the enzyme acts upon
active site
place on enzyme where the substrate attaches or bonds
domain
region on protein function or reaction occurs
cofactors
metal ions
coenzymes
vitamins
examples of homeostasis
body temperature regulation
regulation of acid/base balance or pH
General Composition of Carbohydrates
CH
2
O
Types of carbohydrates
monosaccharides
disaccharides
polysaccharides
monosaccharides
simple or single sugars
pentose sugars
hexose sugars
pentose sugars
5 carbons
ribose (RNA)
deoxyribose (DNA)
hexose sugars
6 carbons
glucose
fructose
galactose
disaccharides
two hexose sugars are joined by dehydration synthesis
sucrose
maltose
lactose
sucrose
glucose + fructose
maltose
glucose + glucose
lactose
glucose + galactose
ploysaccharides
many glucose molecules joined by dehyd. syn
starch
glycogen
cellulose
Author
CLOWE
ID
41949
Card Set
BIO 264 BIOCHEMISTRY
Description
EXAM 1
Updated
2010-10-13T18:14:35Z
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