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EK Bio 1

molec bio + cellular respiration

QuestionAnswer
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
Created by: miniangel918 on 2010-09-30



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