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BIOCHEM |\ 212 |\Exam |\ 2 |\QUESTIONS |\WITH |\
ANSWERS
Ammonium |\ion,amine |\group |- |\CORRECT |\ANSWERS |\✔✔-NH3+, |-NH Hydroxyl |\group |- |\CORRECT |\ANSWERS |\✔✔-OH carbonyl |\group |- |\CORRECT |\ANSWERS |\✔✔C=O a |\chemical |\group |\consisting |\of |\a |\carbon |\atom |\linked |\by |\a |\double |
bond |\to |\an |\oxygen |\atom carboxyl |\group, |\carboxylate |\ion |- |\CORRECT |\ANSWERS |\✔✔Carboxyl |
group: |\Functional |\group |\in |\organic |\compounds |\that |\contain |\a |
carbon |\doule |\bonded |\to |\an |\oxygen |\and |\singe |\bonded |\to |\a |\hydroxyl |\group(-OH) Carboxylate |\ion:the |\negative |\ion |(anion) |\formed |\as |\the |\conjugate |
base |\when |\a |\carboxylic |\acid |\loses |\a |\proton. |\R −COOH ⟶R −COO − +H+ |\Being |\its |\conjugate |\base, |\sodium |\acetate |\mixed |\with |\acetic |
acid |\makes |\a |\useful |\buffer |\solution |\for |\many |\biochemical |\reactions |
where |\a |'mildly |\acidic' |\pH |\of |\4-6 |\is |\desired.
Amide |\group |- |\CORRECT |\ANSWERS |\✔✔the |\N-H |\group |\in |\peptide |
bonds. Amide |\is |\a |\compound |\with |\the |\functional |\group |\that |\consist |\of |
CONR Primary |\amide: |\Nitrogen |\attached |\to |\on |\carbon Secondary |\amide: |\Nitrogen |\attached |\to |\ 2 |\carbon Tertiary |\amide: |\Nitrogen |\attached |\to |\ 3 |\carbon. Thiols |- |\CORRECT |\ANSWERS |\✔✔-SH Sulfides |- |\CORRECT |\ANSWERS |\✔✔-S- Disulfide |- |\CORRECT |\ANSWERS |\✔✔-S-S- 4 |\Classes |\of |\Biomarcomolecules |- |\CORRECT |\ANSWERS |\✔✔1.Proteins
- |\Lipids: |\Membranes,fatty |\acids,cholesterol, |\Eicosanoids
- |\Nucleic |\acids:RNA |\and |\DNA 4.Carbohydrates: |\Table |\sugar,Cellulose,Starch ,Glycogen Enzymes |- |\CORRECT |\ANSWERS |\✔✔Catalyze |\biochemical |
reactions(BIological |\Catalysts)
Elastin-ligaments Keratin-fingernails Protective |\proteins |- |\CORRECT |\ANSWERS |\✔✔Provide |\defense |\against |\invaders |\and |\protect |\from contractile |\proteins |- |\CORRECT |\ANSWERS |\✔✔Do |\mechanical |\work Actine |\and |\myosin-Muscles Kinesin-Vesicle |\transport Isomers |- |\CORRECT |\ANSWERS |\✔✔Compounds |\with |\the |\same |
chemical |\formula, |\but |\different |\structures. Constituiaotnal |\Isomers |- |\CORRECT |\ANSWERS |\✔✔Isomers |\that |\differ |\in |\the |\bonding |\order |\of |\atoms H3C-CH2-OH H3C-O-CH
Stereoisonmers |- |\CORRECT |\ANSWERS |\✔✔Isomers |\that |\have |\atoms |
bonded |\in |\th |\same |\order, |\but |\with |\different |\arrangements |\in |\space Enantiomers |- |\CORRECT |\ANSWERS |\✔✔Mirror |\images |\of |\steroismoers |\that |\cannot |\be |\superimposed(Slide |\ 20 |\Lecture |\ 8 |\for |\example) Diastereoisomers |- |\CORRECT |\ANSWERS |\✔✔Stereoisomers |\that |\are |
not |\mirror |\images(Slide |\ 20 |\Lecture |\ 8 |\for |\example) Hydrophobic |- |\CORRECT |\ANSWERS |\✔✔substances |\that |\will |\not |
dissovle |\in |\water (water-fearing: |\cannot |\H |\bond |\with |\water) Hydrophilic |- |\CORRECT |\ANSWERS |\✔✔Substance |\that |\will |\dissolve |\in |
water |
(water-loving: |\H-bonds |\with |\water) Acid, |\Basic |,neutral |\polar, |\uncharged Four |\classes |\of |\ammino |\acids |- |\CORRECT |\ANSWERS |\✔✔1. |\Nonpolar: |\side |\chains |\are |\alkanes |\and |\arenes(No |\charge)
Formation |\of |\a |\peptide |\bond |- |\CORRECT |\ANSWERS |\✔✔Two |\amino |
acids |\covalently |\linked |\together |\by |\an |\amide |\bond |\aka-peptide |
bond |\form |\a |\dipeptide Protein |\primary |\structure |\ 1 |- |\CORRECT |\ANSWERS |\✔✔Proteins |\are |
written |\N-terminal |\to |\C-terminal |
the |\order |\of |\amino |\acids |\differe |\for |\each |\protein The |\primary |\structure |\determines |\the |\form |\and |\function |\of |\the |
protein Electrostatic |\interactions(Salt |\bridges) |- |\CORRECT |\ANSWERS |\✔✔Ionic |
bond |\between |\acidic |\and |\basic |\side |\chains Ionic |\bonds |\between |\aminio |\and |\carboxyl |\termini Charges |\on |\end |\pull |\each |\other |\different |\ways Hydrogen |\bonds |- |\CORRECT |\ANSWERS |\✔✔Occur |\between |\H-bond |
donors(O-H |\and |\N-h) |\and |\acceptors(O |\and |\N) Oh |\bond |\or |\H3N |+ |\o |\at |\the |\end
Vander |\waals |\forces |- |\CORRECT |\ANSWERS |\✔✔Occur |\between |\all |
atoms C |\or |\CH |\at |\the |\end |(Maybe) Structural |\Amino |\Acids |\1: |\Glycine |- |\CORRECT |\ANSWERS |\✔✔No |
organic |\side |\chain, |\flexible-located |\in |\turns Structural |\Amino |\Acids |\2: |\Proline |- |\CORRECT |\ANSWERS |
✔✔Secondary |\amine(side |\chain |\attached |\to |\Calpha |\and |\backbone |\N) |\forms |\tertiary |\amine |\upon |\formation |\of |\peptide |\bond |\ridged |
structure,found |\at |\the |\end |\of |\the |\helix |\and |\beginning |\of |\turns. Structural |\Amino |\Acids |\3: |\Cysteine |- |\CORRECT |\ANSWERS |\✔✔Thiols(- SH) |\groups |\forms |\disulfide |\bonds |\in |\extracellualr |\proteins,binds |
metals. primary |\protein |\structure |- |\CORRECT |\ANSWERS |\✔✔Covalent |\bonds: Intramolecular |\bonds occuring |\between |\atoms |\of |\amino |\acids,in |\peptide |\bonds |\and |\in |
disulfide |\bonds
Secondary |\structure: |\Beta-strands |- |\CORRECT |\ANSWERS |\✔✔Beta- pleated |\sheets |\are |\made |\of |\up |\Beta-strands. |\A |\Beta-pleated |\sheet |\is |\held |\together |\by |\amide |\groups, |\which
- |\form |\peptide |\bonds |\between |\adjacent |\residues |
2)hydrogen |\bond |\between |\amide |\groups |\on |\adjacent |\strands Disulfide |\bonds |- |\CORRECT |\ANSWERS |\✔✔form |\covalent |\bonds |\that |
stabilize |\protein |\structure |\once |\it |\is |\fold |\into |\a |\tertiary |\structure. Hydrophobic |\Effect |- |\CORRECT |\ANSWERS |\✔✔Side |\chain |\of |\nonpolar |
resides |\exclude |\water |\to |\pack |\together |\in |\the |\center |\of |\the |\protein Two |\types |\of |\functional |\protein |\structures |- |\CORRECT |\ANSWERS |
✔✔Tertiary |\structure: |\Consisits |\of |\single |\polypetide |\chains Quaternary |\Structure: |\Consists |\of |\multiple |\protein |\chains Globular |- |\CORRECT |\ANSWERS |\✔✔forms |\a |\globe-like |\structure, |
typically |\water |\soluble |\as |\hydrophilic |\residues |\are |\on |\the |\surface Fibrous |- |\CORRECT |\ANSWERS |\✔✔Forms |\fibers |\or |\sheet, |\typically |
insoluble |\containing |\small |\hydrophobic |\residues |\that |\pack |\tightly |
together |\in |\layers; |\either |\or |\alpha |\helical |\or |\beta |\sheet Conjugated |\proteins |- |\CORRECT |\ANSWERS |\✔✔Glycoproteins
Lipoproteins Metalloproteins Phosphoproteins Hemoproteins Nucleoproteins Glycoprteins |- |\CORRECT |\ANSWERS |\✔✔Covalently |\bound |\carb(Eg. |
form |\receptors |\on |\cell |\surface) Lippoproteins |- |\CORRECT |\ANSWERS |\✔✔Covalently |\bound |\to |
lipids(eg. |\transport |\cholesterol) Metalloproteins |- |\CORRECT |\ANSWERS |\✔✔Metal |\ions |\for |\structure |
stabilization |\or |\catalytic |\function Phosphproteins |- |\CORRECT |\ANSWERS |\✔✔Covalently |\bound |
phosphate |\groups |\used |\to |\activate |\or |\deactive |\a |\protin |\or |\provide |
binding |\sites |\for |\protein |\attachment Hemoproteins |- |\CORRECT |\ANSWERS |\✔✔Contain |\heme |\groups/porphyrin |\rings(Eg. |\oxygen |\transproters, |\drug |\metabolizing |
enzymes, |\energy |\producing |\enzymes)
3.Symptoms:Skin |\lesions, |\bruising, |\joint |\pain |, |\swollen, |\bleeding |
gum |\with |\tooth |\loss, |\spontaneous |\nasal |\bleed 4.Curable |\with |\proper |\diet: |\eat |\your |\fruits |\and |\vegetables brittle |\bone |\disease(Osteogenesis |\imperfecta) |- |\CORRECT |\ANSWERS |
✔✔1.Dominant |\inhertiance |\from |\only |\one |\parent
- |\Type |\1: |\NOrmal |\collagen |\just |\insuffience |\amounts. |\primarily |
before |\puberty. |\Symptoms:Uncommon |\bone |\fractures, |\birttle |\teeth, |
greying |\of |\sclera, |\loose |\joints, |\weak |\muscles. |\Often |\mistaken |\for |
child |\abuse. - |\Type |\2: |\poor |\amounts |\and |\quality |\of |\collagen. |\Fractures |\occur |
before |\birth, |\severe |\respiratory |\problems Alpha |\keratin |- |\CORRECT |\ANSWERS |\✔✔a |\fibrous |\protein |\found |\in |
hair, |\fingernails, |\claws, |\horns, |\and |\beaks. |\Is |\stabilized |\by |\Hihgh |
Number |\of |\disulfide |\bonds |(S-S) Chaperones |- |\CORRECT |\ANSWERS |\✔✔Protein |\and |\protein |\complexes |\that |\assist |\in |\the |\folding |\of |\other |\proteins |\and |\protein |\assemblies; |
keep |\proteins |\from |\aggregating |\in |\nonfunctional |\units Prions |- |\CORRECT |\ANSWERS |\✔✔1.Proteins |\llcated |\in |\the |\central |
nervous |\system |(Brain) 2.Convert |\their |\alpha-helices |\and |\loop |\region |\to |\Beta |\sheets
- |\Called |\infectious |\agents |\as |\they |\induce |\other |\normally |\folded |
prions |\to |\change |\shape. |\Each |\converted |\protein |\is |\a |\new |\infectious |
agent misfolded |\infectious |\proteins |- |\CORRECT |\ANSWERS |\✔✔1.Result |\of |
prion |\malformation 2.A |\group |\of |\rare |\degenterative |\brain |\disorder |\charcterized |\by |\tiny |
holes |\that |\give |\the |\brain |\a |\spongy |\appearance - |\Affect |\both |\human |\an |\danimals 4.Occur |\ 3 |\ways: |\sporadically; |\hereditary |\dieases; |\transmission |\from |
infected |\individuals |\ - |\Symptoms |\commonly |\include |\perosnallity |\changes, |\psychiatric |
problmes |\such |\as |\depression, |\lack |\of |\coordination, |\and |\or |\unsteady |\gait. Dieases |: |\Creutzfeldt-Jakob |\disease, |\Variant |\Creutzfeldt-Jakob |\diease, |\Gerstamann-Straussleer-Scheinker |\Syndrome, |\Fatal |\Familial |\Insomia, |\Kuru protein |\degradation |- |\CORRECT |\ANSWERS |\✔✔1. |\Degradation |\by |
proteasomes
3.Detergents 4.Organic |\compounds
- |\pH |\change 6.Inorganic |\salts Heat |- |\CORRECT |\ANSWERS |\✔✔Disrupts |\the |\non-covalent |\interactions Mechanical |\agitation |- |\CORRECT |\ANSWERS |\✔✔Foaming/air |\bubbles |
cause |\lack |\of |\water Detergents |- |\CORRECT |\ANSWERS |\✔✔Can |\interact |\with |\hydrophoci |
side |\chains |\and |\unfold |\the |\protein Organic |\compounds |- |\CORRECT |\ANSWERS |\✔✔Polar |\solvents |\can |
disrupt |\H-bonds |(Ehtanol |\can |\precipitate |\bacterial |\proteins |\is |\used |
as |\disinfectant) pH |\change |- |\CORRECT |\ANSWERS |\✔✔Basic |\and |\acid |\side |\chains |
change |\charge |\disrupting |\salt |\bridges(Milk |\becomes |\acidic |\over |
time |\as |\bacteria |\convert |\lactose |\ot |\lactic |\acid |\causing |\the |\protein |\to |\coagulate) Inorganic |\salts |- |\CORRECT |\ANSWERS |\✔✔at |\high |\concentrations |\and |
disrupt |\salt |\bridges
Enzyme |- |\CORRECT |\ANSWERS |\✔✔Biologoical |\catalyst(Protein |\or |
RNA). |\Enzyme |\names |\ends |\in |\ase. |\Typically |\named |\after |\the |
substrate |\of |\the |\reaction |\that |\it |\catalzyes. Substrate |- |\CORRECT |\ANSWERS |\✔✔reactant |\of |\an |\enzyme-catalyzed |
reaction Turnover |\number |- |\CORRECT |\ANSWERS |\✔✔number |\of |\substrate |
molecules |\an |\enzyme |\converts |\to |\a |\product |\per |\second Cofactor |- |\CORRECT |\ANSWERS |\✔✔nonprotein |\substacne |\that |\binds |
to |\the |\protein |\and |\is |\required |\for |\catalysis Coenzyme |- |\CORRECT |\ANSWERS |\✔✔Organic |\cofactors |\typically |
found |\in |\redox |\enzymes Apoenzyme |- |\CORRECT |\ANSWERS |\✔✔protein |\minus |\its |\cofactor/enzyme Holoenzyme |- |\CORRECT |\ANSWERS |\✔✔catalytically |\active |\enzyme |
containing |\the |\apoenzyme |\with |\its |\cofactor/coenzyme
transferases |- |\CORRECT |\ANSWERS |\✔✔transfer |\functional |\groups |
from |\one |\substrate |\to |\another hydrolyses |- |\CORRECT |\ANSWERS |\✔✔Catalyze |\hydrolysis |\of |
substrates(water |\lysis) Isomerases |- |\CORRECT |\ANSWERS |\✔✔catalyze |\the |\isomerization |\of |
substrate(rearranges |\bonds |\of |\the |\substrate) Lyases |- |\CORRECT |\ANSWERS |\✔✔catalyze |\the |\elimination |\of |
functional |\group |\by |\forming |\a |\double |\bond |\or |\breaking |\a |\double |
bond Ligases |- |\CORRECT |\ANSWERS |\✔✔Catalyze |\bond |\formation |\couple |
with |\ATP |\hydrolysis(which |\provides |\the |\energy |\of |\the |\bond |
formation) Oxidoreducatase |- |\CORRECT |\ANSWERS |\✔✔Catalyze |\the |\oxidation |\or |
reducation |\of |\a |\substrate Requires |\a |\coenzyme |\for |\catalysis. |\Oxidation |\and |\reduction |\happen |
simultaneously. |\If |\the |\susbtrate |\is |\to |\be |\oxidized, |\then |\the |
coenzyme(Not |\the |\protein)is |\reduced. |\If |\the |\substrate |\gets |\reduced, |\then |\the |\coenzyme |\is |\oxidzed.
Subclass: |\Dehydrogenases-remove |\ 2 |\hydrogen |\atoms |\from |\a |
substrate |\to |\form |\doublebondl |\Requires |\FAD |\or |\NAD+ |\as |\coenzyme |
FAD |\removes |\H |\from |\ 2 |\covalently |\bonded |\carbon |\atoms |\to |\form |\an |\alkene |\NAD |\removes |\H |\from |\the |\covalently |\bonded |\OH |\and |\C |\to |
form |\a |\carbonyl |\group Transferases |- |\CORRECT |\ANSWERS |\✔✔Catalyze |\the |\transfer |\of |\a |
fuctional |\group. |(Amino |\or |\phosphoryl)Between |\substrates Subclasses: Kinases-transfers |\a |\phosphoryl |\gorup(-POsubscript3^2-)between |
substrates Transaminase-transferes |\an |\amino |\group |(-NHsubscipt3^+1)between |
susbtrates Hydrolases |- |\CORRECT |\ANSWERS |\✔✔Catalyze |\the |\hyrdolysis |\of |\a |
substrate.(Means |\water |\splutting-substrate |\bonds |\break |\by |\adding |
an |\H |\to |\the |\product |\on |\one |\side |\of |\the |\broken |\bond |\and |\an |\OH |
group |\to |\the |\other |\product) Subclasses: Lipases |- |\hydrolyze |\ester |\bonds |\in |\lipids Proteases |- |\hydrolyze |\peptide |\bonds |(backbone |\amides)
