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78 Cards in this Set

  • Front
  • Back
What does biochemistry aim to describe?
At the molecular level structures, mechanisms and chemical processes shared by all organisms and to explain the molecular logic of life.
Health (as definted by the biochemical point of view)
situation in which all of hte intra and extracellular reactions that occur in the body are in perfect harmony
Disease (as definted by teh biochemical point of view)
situation that reflects abnormalities in biomolecules and/or imbalances in biochemical reactions
Level of organization in the human body
atoms-->molecules-->marcomolecules-->organelles-->cells-->tissues-->organs
what macromolecules can be found in cells?
lipids (cell membranes)

proteins, nucleic acids, carbohydrates (organelles)
Essential elements for life
H, C, O, S, N, P
Five essential ions for life
Na
K
Cl
Ca
Mg
Iodine deficiency diseases
-endemic goiter
-dwarfism
-mental retardation
iron imbalance syndromes
too much iron: Hemochromatosis-->liver cancer

too little iron: anemia --> low levels of healthy RBC's or Hemoglobin
copper imbalance syndromes
too much Cu: wilson's disease

-Kayser-Fleisher ring (brown area around cornea)
-slurred speech
-difficulties in swallowing
-tremor of arms and legs
-possible psychiatric issues

TOO LITTLE IRON: Menkes' Syndrome: Sparse, kinky hair; physical or mental retardation; progressive deteroration of the brain
Wilson disease
result of too much copper

Kayser-Fleisher Ring (brown area around cornea)
-slurred speech
-difficulties in swallowing
-tremor of arms and legs
-possible psychiatric issues
Kayser-Flesisher ring
Wilson's disease

results from too much Copper

brown area around the cornea
-slurred speech
-difficulties in swallowing
-tremor of arms and legs
-posisble psychiatric issues
Menkes' syndrome
result of too little copper.

-sparse, kinky hair
-physical (and possibly mental) retardation
-progressive deteroration of the brain
hemochromatosis
result of too much iron

liver cancer
anemia
result of too little iron

low levels of healthy RBC's or hemoglobin
Ionic bond
complete transfer of electrons from one atom to another, forming oppositely charged atoms that electrostatically attract one another
polar covalent bond
a covalent bond that has an uneven distribution of electronic density due to an unequal sharing of bonding electrons

ex. H2O
non-polar covalent bond
a covalent bond that has an equal electronic density due to an equal sharing of bonding electrons

ex. O2, H2, or Methany (CH4)
electronegativity
a mathematic parameter that measures the force with which an atom attracts electrons that is shares in a chemical bond with another atom
electronegativity of C, H, N, and O.
O, N are more electronegative than C,H.
Stereochemistry
study of the 3D structure of molecules

-each organic molecule has a unique 3D shape that determines its biological function
Isomer
different compounds with the same molecular formula

important because they can have different chemical, physical and biological properties
Consitutional isomer
isomers whose atoms have different CONNECTIVITY
stereoisomers
isomers that have the SAME CONNECTIVITY but differ in the ARRANGEMENT of their atoms in SPACE
light detection in the human eye
Vitamin A (trans-RetinOl)-------> Cis-RetinOl (via isomerization)

Cis-RetinOL-----> Cis- RetinAL (via oxidtaion)

Cis-retinAl--->trans-retinAL (via isomerization)

Trans-retinAl--> rhodopsin (photoreceptor)---> Brain (so you can see in the light!)

if there is no light, Cis-retinAl cant be isomerized into Trans-retinAL, and you would have nyctalopia (night blindness)
night blindness
nyctalopia

caused by vitamin A deficiency
nyctalopia
night blindness caused by vitamin A deficiency

normal vision is strong in light, but loss of vision in the dark or dim light.
Chiral atom
A chiral atom is an atom in a molecule that is attached to 4 different atoms/groups
mirror images
everything has a mirror image, and some mirror images are superimposable, and others are not.

superimposable mirror image= ACHIRAL

non-superimposible mirror image=CHIRAL

BIOMOLECULES ARE CHIRAL!!!
are biomolecules chiral or achiral?
CHIRAL!
Chiral
mirror images are not superimpossible
achiral
mirror images are superimposable
enantiomers
chiral stereoisomers that have identical chemical and physical properties, but different biological and optical ones.........

two mirrow images?
is life mostly chiral or achiral?
right or left handed?
LIFE IS CHIRAL AND MOSTLY LEFT-HANDED
amino acids
contains an amino group(NH3) and a carboxyl ground (Coo-)
alanine
ala
hydrophobic
non-polar
alanyl
arginine
arg
hydrophilic
basic
arginyl
asparganine
asn
hydrophilic
neutral
asparaginyl
aspartic acid
asp
hydrophilic
acidic
aspartyl
cysteine
cys
hydrophilic
neutral
cysteinyl
glutamine
gln
hydrophilic
neutral
glutaminyl
glutamic acid
glu
hydrophilic
acidic
glutamyl
glycine
gly
hydrophilic
neutral
glycyl
histidine
his
hydrophilic
basic
histadyl
isoleucine
ile
hydrophobic
non-polar
isoleucyl
leucine
leu
hydrophobic
non-polar
leucyl
lysine
lys
hydrophilic
basic
lysyl
methionine
met
hydrophobic
non-polar
methionyl
phenylalanine
phe
hydrophobic
non-polar
phenylalanyl
proline
pro
hydrophobic
non-polar
prolyl
serine
ser
hydrophilic
neutral
seryl
threonine
thr
hydrophilic
neutral
threonyl
tryptophan
trp
hydrophobic
non-polar
tryptophanyl
tyrosine
try
hydrophobic
neutral
tyrosyl
valine
val
hydrophobic
non-polar
valyl
uncommon amino acids
derived from common AA; produced by POST TRANSLATIONAL MODIFICATION (modification of parent AA after the protein has been synthesized in the body)

1. Hydroproline (from Proline)
2. Hydrolysine (from lysine)
3. Thyroxine (from Tyrosine)
3 uncommon amino acids
hydroproline (from proline)
hydrolysine (from lysine)
thyroxine ( from tyrosine)
What are T3 and T4? What are their roles in the body biologically?
T3 and T4 are made from tyrosin + iodine. Thyroid hormone is a mixture of T3 (80%) and T4(20%)

T3= 2 tyrosine + 3Iodine
T4=2 tyrosine + 4 Iodine...usually converted to T3 by loss of a I

T3: metabolically active thyroid hormone:
increases BMR, heart rate and growth
What is the principle of L-dopa therapy for parkinson's disease?
dopamine can't cross the BBB. When there are low levels of dopamine in the brain)(parkinson's disease), L-dopa is taken because it is able to cross the BBB after it gets into the systemic circulation. once L-dopa crosses the BBB it converts into dopamine
What AA is the precursor of polyamines? What's the biological role of polyamines?
Arginine produces polyamines.

polyamines:
-DNA synthesis
-Growth factor in cells
-modulate ion channels
What AA is a precursor for Histamine? What does Histamine do?
Histadine --->histamine

histamine is important in immune responses and allergic reactions:
-neurotransmitter
-triggers inflammatory response
-increase capillary permeability to WBC's
What are the Essential Amino acids?
what does essential mean?
Essential=required in the diet because the body can't synthesize them.

alanine//histidine//isoleucine//leucine//threonine//lysine//methionine//phenylalanine//tryptophan//valine
amphoteric (amphiprotic)
having the capacity to act as both an acid and a base
what is a biological buffer>
compound or system of compoudsn that can either accept or donate H+ ions, depending on the acidic/basic character of the solution they're in
homeostatic
living organisms are self-regulating...theri life depends on HOMEOSTASIS= ability to maintain internal equilibrium by adjusting their physiological processes
homeostatic systems in the body
1. bicarbonate buffer system (lungs=fast)
2. phosphate buffer system (kidneys=slow)
3. protein buffer system
bicarbonate buffer system
H+ + HCO3-->H2CO3-->CO2 (d) (H20 is given off)--->CO2 (g) in the lungs
hypoventilation
acidosis
ph<7.35
[H+]>[HCO3]

usually from diseases affecting the lungs
hyperventillation
Alkalosis
pH>7.45
[H+]<[HCO3]


usually from stress, anxiety, fever, etc.
peptide bond
bond joining two amino acids by eliminating a molecule of water between a carboxyl group from one AA and an amino acid group from the other
peptide hormones in the body
oxytocin: stimulates breast feeding and labor
-induces behavioral responses (social recognition, emotional attachment, anxiety, trust)

2. vassopressin (ADH) -regulates BP, antidiuretic

3. Carosine (beta-alanyl-L-hitidine): in muscle and brain tissues, powerful antioxidant
oxytocin
a peptide hormone found in the body

stimulates breast feeding and labor

induces behavioral responses:
-social recognition
-emotional attachment
-anxiety
-trust
Vasopressin (ADH)
peptide hormone in the body

regulates BP
antidiuretic
carnosine (beta-alanyl-L-histadine)
peptide hormone in the body

found in muscle and brain tissues
-a powerful antioxidant
hydrophilic
"Water loving"
soluble in water due to ionic or polar covalent bonds
hydrophobic
"water fearing"
insoluble in water due to non-polar covalent bonds
amphipathic
partially hydrophilic and hydrophobic due to simultaneous presence of ionic and/or polar covalent and non-polar covalent bonds
principle of water solubility
"like dissolves like"
polar=dissolves polar
non-polar=dissolves non-polar

electrostatis attraction of opposite charges by ion-dipole and dipole-dipole interacctions: positive dipole of water attracts a negative ion or a negative dipole of another molecule