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molec bio + cellular respiration

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hydrogen bonding in water allows..   it to maintain liquid state in the cellular environment  
lipids   any biological molecule that has low solubility in water and high solubility in nonpolar organic solvents; hydrophobic  
what are the six groups of lipids?   fatty acids, triacylglycerols, glycolipids, terpenes, steroids, phospholipids  
fatty acids   building blocks of most complex lipids; long chains of carbons with carboxylic acid at one end  
triacylglycerols   aka triglycerides (fats and oils) constructed from three C glycerol with having a carbon chain; STORE ENERGY AND PROVIDE THERMAL INSULATION AND PADDING  
phospholipids   built from glycerol backbone but a SERVE AS STRUCTURAL COMPONENT OF MEMBRANES; polar phosphate replaces one of the fatty acids to create an amphipathic molecule  
steroids   four ringed structures that include hormones, vitamin D, and cholesterol (also membrane component); REGULATE METABOLIC ACITIVITIES  
eicosanoids   SERVE AS LOCAL HORMONES; include prostaglandins, thromboxanes, and leukotrienes  
proteins   built from a chain of amino acids linked together by peptide bonds  
essential amino acids   humans have 10 - meaning humans cannot manufacture these 10 and must be ingested  
non polar R groups   glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, proline  
polar R groups   serine, threonine, cysteine, tyrosine, asparagine, glutamine  
acidic R groups   aspartic acid, glutamic acid  
basic R groups   lysine, arginine, histidine  
primary structure   number and sequence of amino acids in polypeptide chain  
secondary structure, alpha helix and beta pleated sheets   contribute to conformation of protein  
alpha helix   conformation of single protein chain (twisted into helix) which are reinforced by hydrogen bonds between carbonyl oxygen and hydrogen on amino group  
beta pleated sheet   connecting segments of two strands of sheet can lie parallel or anti-parallel which are reinforced by hydrogen bonds between carbonyl oxygen and hydrogen on amino group  
tertiary structure   3D shape of peptide chain created by (1) covalent disulfide bonds between 2 cysteine (2) electrostatic interactions btw acidic and basic side chains (3) hydrogen bonds (4) VDW forces (5) hydrophobic side chains pushed away from H2O  
quaternary structure   shape when two or more polypeptide chains bind together, depends on same five forces that tertiary structure does  
globular proteins   function as enzymes, hormones, membrane pumps and channels, membrane receptors, intercellular and intracellular transport and storage, osmotic regulators, immune response - antibodies  
structural proteins   made of long polymers which maintain and add strength to cellular and matrix structure (collagen, microtubules)  
glycoprotein   proteins w/ carb groups attached  
cytochromes   proteins which require prosthetic heme grope in order to function  
carbohydrates   aka sugars or saccharides, made of carbon and water  
glucose   6 carbon carb, most commonly occurring, accounts for 80% of carbs absorbed by humans, exists in aqueous sol'n favoring ring form  
alpha-glucose   OH group on anomeric carbon (Carbon 1) and the methoxy group (Carbon 6) are on opposite side of carbon ring  
beta-glucose   OH group and CH3OH group are on the same side  
glycogen   alpha linked polymerized glucose found in all animal cells as a way to store glucose  
starch   another alpha linked glucose, comes in two forms amylose and amylopectin  
cellulose   beta linked polymerized glucose, animals cannot digest beta linkages only bacteria can digest  
nucleotide   composed of a five carbon sugar, nitrogenous base, and a phosphate group  
most common nitrogenous bases   adenine, guanine, cytosine, thymine, and uracil  
phosphodiester bond   joins the nucelotides by creating bond between phosphate group of one nucleotide and the 3rd carbon of the pentose of the other nucelotide  
adenine and thymine form how many H bonds   two  
cytosine and guanine form how many H bonds   three  
ATP   adenosine triphosphate, nucleotide that acts as source of readily available engery for the cell  
cAMP   cyclic AMP, important component of second messenger systems  
coenzymes involved in the Kreb's cycle   NADH and FADH2  
minerals   dissolved inorganic ions inside and outside the cell; assist in transport of substances entering/exiting cell; can combine and solidify to give strength to matrix; can act as co-factors assisting enzyme or protein function  
enzymes   globular protein, function as catalyst to lower energy of activation for bio rxn and increasing rate of rxn; exhibit saturation kinetics  
lock and key theory   active site of the enzyme has a specific shape like a lock that only fits a specific substrate (the key)  
induced fit enzyme model   the shape of both the enzyme and substrate are altered upon binding which increases specificity and helps rxn to proceed; in cases with multiple substrates, the enzyme can orient substrates relative to each other to create optimal conditions for the rxn  
saturation kinetics   where as the relative concentration of substrate increases, the rate of rxn also increases, but to a lesser and lesser degree until a max rate has been achieved  
factors affecting enzyme rxns   substrate conc, temp, pH, cofactors  
cofactor   non-protein component required by enzymes to reach optimal activity (coenzymes or metal ions)  
coenzyme   organic molecules that help enzymes obtain optimal activity; divided into two types - cosubstrates and prosthetic; eg: vitamins  
cosubstrate   reversibly bind to specific enzyme & transfer some chem group to another substrate and reverted back to original by another enzymatic reaction; eg: ATP  
prosthetic group   remain covalently bound to enzyme through reaction; eg: heme  
temperature and enzymatic rxns   increased temp will increase rxn rate until enzyme is denatured, then it rxn rate drops dramatically  
pH and enzymatic rxns   optimal pH depends on enzyme  
types of enzyme inhibition   irreversible, competitive, non-competitive  
irreversible inhibitor   agent that binds covalently to enzymes to disrupt their function; tend to be highly toxic  
competitive inhibitor   agents which compete with the substrate by binding reversibly with noncovalent bonds to the active site, can be overcome with increasing the substrate concentration, raises apparent Km but Vmax remains same  
noncompetitive inhibitor   agents which bind noncovalenty to an enzyme at a spot other than the active site and change the confirmation of enzyme, will lower Vmax but the affinity of the enzyme remains the same (Km)  
Km   Michealis constant, substrate conc at which the rxn rate is equal to 1/2 the Vmax, good indicator of enzyme's affinity to substrate  
four methods of enzyme regulation   proteolytic cleavage, reversible covalent modification, control proteins, allosteric interactions  
proteolytic cleavage   enzymes become irreversibly active when after specific peptide bonds cleaved on its zymogen/proenzyme  
reversible covalent modification   activated/deactivated by phosphorylation or addition of some other modifier (often accomplished by hydrolysis)  
control proteins   protein subunits that associate with certain enzymes to activate/inhibit their activity; eg calmodulin or G-proteins  
allosteric regulation   molecules that regulate enzyme activation/inhibition by causing conformational change (eg feedback inhibition); not necessarily noncompetitive inhibitors; exhibit atypical kinetics  
negative feedback   one of the products downstream inhibits the enzyme early in the reaction  
positive feedback   one of the products returns to activate the enzyme (occurs less often then negative)  
positive cooperativity   after the first substrate changes the shape of the enzyme, the other substrates bind more easily (like oxygen on hemoglobin)  
categories of enzymes   oxidoreductases, transferases, hydrolyses, lyases, isomerases, ligases  
metabolism   all cellular chemical rxns consisting of anabolism (molecular synthesis) and catabolism (molecular degradation)  
three stages of metabolism   (1)macromolecules broken down to their constituent parts (2)constituent parts oxidized to acetyl CoA/pyruvate/other metabolite forming some ATP and reduced coenzymes(no O2) (3)if O2 available, metabolites go into citric acid cycle & oxidative phosphor  
respiration   energy acquiring stages of metabolism, can be anaerobic or aerobic  
anaerobic respiration   respiration where oxygen is not required, includes glycolysis and fermentation  
glycolysis   series of rxns that breaks 6-C glucose molecule into two 3-C molecules of pyruvate  
6-C stage of glycolysis   expends two ATPs to phosphorylate the molecule  
3-C stage of glycolysis   synthesizes 2 ATP with each 3 carbon molecule  
glycolysis products   4 ATP + 2 pyruvate + 2 NADH  
glycolysis reactants   glucose + 2 ATP + 2 NAD+  
glycolysis reaction   glucose + 2 ATP + 2 NAD+ --> 2 pyruvate + 4 ATP + 2 NADH  
irreversible steps of glycolysis   (1) glucose to glucose-6-phosphate (phosphorylated glucose) - assists facilitated diffusion mech which transports glucose into the cell (2) fructose-6-phosphate to fructose-1,6-bisphosphate at the expense of ATP  
substrate level phosphorylation   formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to using the energy from diffusion)  
fermentation   glycolysis + reduction of pyruvate to etOH or lactic acid + oxidation of NADH back to NAD+  
when does fermentation take place   when cell/organism either unable to use the energy from NADH and pyruvate or has no oxygen to do so  
why does NAD+ need to be restored (in fermentation)   NAD+ acts as a coenzyme in glycolysis  
where does glycolysis take place   cytosol  
aerobic respiration   requires oxygen, produces 36 net ATP (including glycolysis)  
NADH brings back how many ATP   2 - 3  
FADH2 brings back how many ATP   2  
Kreb's cycle   aka citric acid cycle, takes place in mitochondrial matrix to produce 1 ATP, 3 NADH, and 1 FADH2 (also substrate level phosphorylation), loses two carbons as CO2, and reproduces oxaloacetic acid  
Acetyl CoA   coenzyme which transfers 2 carbons from pyruvate to the 4-C oxaloacetic acid to begin the Kreb's cycle  
fatty acids role in respiration   tryglyceride - glycerol converted to PGAL and fatty acids converted go acyl CoA to acetyl CoA  
proteins role in respiration   deaminated in liver so amino acids can be converted to pyruvic acid or acetyl CoA or other steps in the Kreb's cycle  
electron transport chain   series of proteins (including cytochromes with heme) in the membrane of mitochondrion where electrons are passed down to ultimately be accepted by oxygen to create a proton gradient  
oxidative phosphorylation   producing ATP using a proton motive force pushing protons through ATP synthase  
overall respiration rxn   glucose + O2 --> CO2 + H20  


   





 
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Created by: miniangel918 on 2010-09-30



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