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- charge-induced, dipole-induced
- non-polar molecules with either a charged molecule or a polar molecule
- dispersion
- 2 non polar molecules (2 rings).. vanderwaals forces
- AA with side chains containing -0H groups
- serine, threonine, tyrosine
- AA with side chains containing acidic groups or their amides
- aspartic acid, asparagine (asn), glutamic acid, glutamine (gln)
- AA with aliphatic side chains
-
*consist of C and H only*
glycine, alanine, valine, leucine, isoleucine - AA with side chains containing basic groups
- arginine (guaunido group, lysine, histidine
- AA with side chains containing aromatic rings
- histidine, phenalanine, tyrosine, tryptophan
- AA with side chains containing sulfer atoms
- cystEine, methionine
- AA with side chains containing Imino Acids
- proline - hydrophobic
- 7 groups that can become ionizable (charged)
- cysteine, arginine, lysine, histidine, aspartic acid, glutamic acid, tyrosine
- Secondary Amino Acids
- CystIne, hydroxyproline, hydroxylysine, phosphoserine, phosphothreonine, phosphotyrosine
- Acid Dissociation Constant
- Ka = (conj base) (H+) / (undissociated acid HA)
- pH =
- -log[H+]
- pKa =
- -logKa
- pH = pKa..
-
+ log [conj base]/[undis acid]
( A-/HA ) - prosthetic group
- a tightly bound, non-polypeptide substance required for the biological activity of the protein
- Apoprotein
- a protein without its characteristic prosthetic group (globin w/o heme)
- Holoprotein
- A complete protein (with prosthetic group)
- Allosteric interactions
- interactions between spatially distinct sites that are transmitted by conformational changes in a protein (sometimes across subunits)
- Allosteric effectors
- interact with protein (at a site distinct from the substrate site) to induce conformational changes and affect binding of substrate
- 4 principal blood buffer systems
-
1. bicarbonate
2. hemeglobin
3. plasma proteins
4. phosphate
*all pka values near 7.4 EXCEPT bicarb. - High PCO2
-
- CO2 escape decreases
- Hypoventilation
**emphysema, oversedation, head trauma
- respiratory acidosis - Low pCO2 (below 40)
-
- CO2 escape increases
- hyperventilation
** hypoxia, nervousness/anxiety
- respiratory alkilosis - Low HCO3- (less than 24)
- - accumulation of H+
- ** low HCO3-
-
- accumulation of H+ (loss of HCO3)
** diabetic ketoacidosis, lactic acidosis, diarrhea
- metabolic acidosis - High HCO3
-
- loss of H+, accumulation of HCO3
**vomitting (loss of acidic fluid), aldosteroidism (excess renal secretion of H, K, Cl)
- metabolic alkilosis - CORRECTION of acid-base abnormalities
- Abnormal pH returned to normal by changing the component PRIMARILY affected
- COMPENSATION of acid-base abnormalities
- system not primarily affected is responsible for returning pH toward 7.4 but does NOT necessarily involve return of pCO2 or HCO3- to normal values!
- Anion Gap
-
[Na+] + [K+] - [Cl-] - [HCO3-]
142 - 104 - 24 = 14 meq/L
Even if the pH is normal, if there are anions in excess, there is a metabolic disorder - Apoenzyme
- A cofactor (loosely bound, unlike prosthetic groups) -requiring enzyme without its cofactor bound
- Holoenzyme
- an enzyme with its cofactor bound
- Cofactors are
-
vitamins or derivatives of vitamins
compounds that are required for normal growth but are NOT synthesized by the huamn body
in direct participation in group transfer reactions
stabilizers of ES complex - Homotropic Effectors
-
+ effect: binding of S to active site of one subunit causes a conformational change in another subunit
- effect: binding of S to one site causes other sites to become lower affinity - Heterotropic effectors
-
+ effectors: binding at a separate site causes the active sites to have a higher affinity for substrate (R to L shift!)..higher velocity at any substrate concentration
- effectors: binding at separate site decreases the affinity for the first S binding (L to R shift.. lower velocity at any substrate concentration) - Isozymes
- enzymes that catalyze the same chemical reaction but differ in their physicochemical and kinetic properties
- After myocardial infarction.. the enzymes peak at different times...
- CK (creatine kinase) first, then AST (aminotransferase), then LDH (lactate dehydrogenase)
- Transferase
-
transfers a functional group from one compound to another compound
- a KINASE.. transfers PO4 groups - Hydrolase
- breaks bonds by the addition of H20
- Dehydrolase
- Remove H2O from compound(s)
- Isomerase
- catlayzes the formation of isomers of a compound (configurational change)
- Ligases
- Makes bonds USING ENERGY (ATP)
- 2 classes of enzymes that can break bonds
- hydrolases, and lysases
- 2 classes of enzymes that can make BIG molecules (make bonds)
- transferases and ligases
- Hemiacetal
- formed by the reaction of an aldehyde + alcohol
- hemiketal
- formed by the reaction of a ketone + alcohol
-
blood group antigens
cell surface antigens
components of ECM; has more sugar, less protein -
glycolipids
glycoproteins
proteoglycans - Lipid-Soluble Vitamins
-
- retinal (A): night blindness
- cholecalciferol (D): rickets
- alpha-tocopherol (E): hyporeflexia, ataxia
- phylloquinone (K): hypothrombinemia, hemorrhagic dease - Thiamine
-
B1
Thiaminie Pyrophosphate (TPP
C-chains
beri-beri, and wernicke-korsakoff syndrome (iunduced by gastric bypass surgery) - Riboflavin
-
B2
FAD, FMN
H
Scaly dermatitis, glossitis of tongue, chlilosis - Niacin
-
* can synthesize from tryptophan *
B3
NAD
H
Pellagra (the 3 Ds) - dementia, dermatitis, diarrhea = DEATH - Pantothenate
-
B5
CoA
C-chains - Pyridoxal
-
B6
Pyridoxal phosphate
N
rare (iunduced by isoniazids..given for Tb) - Folate
-
B9
tetrahydrofolate
C chains
megaloblastic anemia, NEURAL TUBE DEFECTS - Cobalamin
-
B12
C chains
Pernicious anemia - Biotin
-
H
covalently attached to carboxylases
CO2
rare.. dermatitis & neurological problems.. RAW EGGS! - Ascorbate
-
C
H
Scurvy - Chemical work
- energy for macromolecule construction and heat
- Transportation
- moves ions and other materials across membranes
- Mechanical work
- it is the thing that makes your msucles move
- isohydric transport
-
transport of C02 with minimal change in pH... it is augmented by the ability of RBC membranes to exchange HCO3- for Cl-
otherwise HCO3- would build up inside the RBC and would oppose more conversion of CO2 to HCO3-