C/P Section Bank

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Intensity of Uniform Electric Field
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How to solve for energy in Joules when given Power and time/duration?Power x pulse duration (time)What type of reaction is proteolytic cleavage?hydrolysis reactionclassic calorimetryBomb calorimetry Measure temp change of the cover to ID sp properties of the sampleBond dissociation EnthalpyThe enthalpy change required to break a covalent bond with all species in the gaseous stateWith photons, how can bonds be broken?Photon energy must be larger than bond energy in order break the bond.thin lens formula1/o + 1/i = 1/fKinetic Energy of a photoelectronKEmax = hf - work functionIn an SN1 reaction, what will form the most stable carbocation and why?Tertiary>Secondary> primary The more EDG you have to stabilize the positive charge (wants e-) the happier the carbocation will be Alkyl groups have an E- donating effect, will 'push' e- towards small positive charge on the cationIn an SN2 reaction, what will form the most stable carbocation and why?Primary> SecondaryCarbocationspositively charged species with a full positive charge on carbonReaction between an amine and excess carboxylic acid will producebyproduct. Of an acidic carboxylic acid and excess unreacted starting material will be acidicExtraction with aqueous baseWill hydrolyze and extract both onto aqueous layer, leaving neutral amine in either layerAnhydrideA functional group containing two carbonyls separated by an oxygen atom (RCOOCOR); often the condensation dimer of a carboxylic acid.In addition of bases, would amide move phases?No, because they would be in the organic phase stillOhms lawV=IRRatio of sound intensitiesImax=/Imin measured in 10^x Eg. Max is 80 db, min is 30 db > I0 x 10^8 / I0 x 10^3 = 10^5What does it mean when the voltmeter is reading 0?Voltage difference between those points are 0, meaning they are teh same voltageWhen resistors are in series, is their current equal?Yes based on properties of resistors in series.Phosphatidesany of a class of compounds that are fatty acid esters of glycerol phosphate with a nitrogen base linked to the phosphate group.Can Liposomes be easily detected ?No, they don't absorb visible light and many molecules absorb UV lightKinetic controlThe preferred product/major output product of the reaction is the one that is formed most quickly and have the lowest activation energy Largely grouped with irreversible reactions Mixing will cause instabilityThermodynamic controlPreference for more stable product, lower free energy. No matter what product forms first, there is a lower energy state product that can be formed, then ill be formed and be the major species in solution. Grouped with reversibility., ability to form more energically stable upon mix if can achieve stable product through mixing, it is thermodynamicFree energy of the reaction Delta G'o is related toKeq = [Product]/[reactant] As Delta G'o= -RTln(Keq) Substitute Answer will be e^([product]/[reactant])What is the electronic configuration of the Co(II) center found in vitamin B12[Ar]3d7 (takes off the 4s electrons) because of the two e- removed from the atom with the (II) indicationWhich cation is most likely to be found in place of Fe(II) in the square planar binding domain of hemoglobin?Co2+ (closely related to Fe2+ b/c it's a transition metal and can support a square planar coordination environment)Kinasean enzyme that catalyzes the transfer of a phosphate group from ATP to a specified molecule. Is a subset of transferaseOxidoreductasecatalyze transfer of electrons or hydrogen ionsHydrolasegeneral term for enzymes that catalyze a hydrolytic cleavage reactionDoes conjugation lowers or increases energy?Lowers Energy and wavelength are inversely proportional according to E= hc/lambda Lower energy = greater wavelength = active in UV-visible spectroscopy = more detectableWhat product is highly favored in an equilibriumWhen it is more stable, through resonance, increases detectabilityMichaelis-Menten Equationv = (vmax [S])/(Km + [S])How to determine km1/2vmax = kmHydrophobic amino acidsAlanine, Valine, Isoleucine, Leucine, Methionine, Phenylalanine, Tyrosine, TryptophanNon-polar Amino acidsGlycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, ProlineAlbuminprotein in blood; maintains the proper amount of water in the blood Mobilizes proteins and lipids in serumDeprotonation of reacting water will make it more___; reactive towards the ____ carbonyl atom of the amide functional groupNucleophilc ; electrophilic Makes water have a negative chargeWhat happens when you hydrolyze a peptide bondUse water to conduct nucleophilic attack on an electrophilic carbonyl carbonBetter nucleophile will have a +/- charge?NegativeBetter electrophilic will have a +/- charge?PositiveWhat is the least interactive side chain, and it's purpose?Alanine and GLycine, (not charged, polar, aromatic, or sterically hindered) Replacing Glycine with alanine in an active site will reduce interaction of the side chain with other active site componentsWhen peptide bonds are hydrolyzed through substitution reaction, it attacks ____ carbon atom of the peptide bond. What structure results?SP2 hybridized; results in a sp3 hybridized tetrahedral intermediate; the double bond between carbon and oxygen becomes a single bond, and the e- are pushed onto oxygen atom giving it a negative charge. This is unstable and the double bond reforms shortly after and the C-N bond breaks SP2 > Sp3 > SP2What type of bond is cleaved by lysozymeGlycoside , which is a special type of acetyl linkage in an oligosaccharide