5566880 Biology Lecture Notes I

7/25/2019 5566880 Biology Lecture Notes I

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Lecture Notes

I. Scientific MethodA. Inquiry Based based on observationB. Proceeds logically & seriallyC.

Initiated by observationD. Steps:1. Observation of the action/change/phenoena/etc!2. "epeatability is the observed phenoena regular/repeatable#

i. Only if repeatable is it possible to scientifically study the behavior3. $echanis %o does it or'#4. %ypothesis: If action is repeatable & echanis observed select hypothesis to test

i. Principle of Parsiony the choice of the easiest hypothesis to test first (Occa)s

"a*or+5. Before e,perienting ap out the possible outcoes

i. %ypotheses:

a! -rong choose another e,perientb! "ight hypothesis ay be a possible e,planation

6. By nature science can disprove but cannot provei. .here are only increasing probabilities of truth

E. .heory as close to scientific truth s is possibleII. Chemical Foundations

A. toic .heory protons (0+ neutrons electrons (2+1. Proton count 3 atoic nuber2. 4lectrons their arrangeent in discreet outer shells dictate the ato)s cheical

properties3. toic ass: protons 0 neutrons (3 baryons 5heavy particles6+ (electrons have little

ass+4. 4ach proton 0 neutron 3 1 7alton or toic $ass 8nit5. Isotope ato ith the sae nuber of protons but differing nubers of neutrons:

neutron count doesn)t change the cheical properties of the eleent as they)re

deterined by the electron arrangeent and electron arrangeent is deterined by the

proton counti. $ass 9 3 single ato eight toic -t 3 average of all naturally occurring isotopesii. 1;

eutrons 3 1; Protons 3 a0>a@+

i. Strength of tendency to for ionic bonds dictated by distance fro center of period

tbl!4. Ionic bonds are not olecules instead for crystals (due to utual attraction of all 0

and atos aongst each other+D. =ovalent Bonds bonds sharing electrons in outer levels not gaining or losing electrons

1.

Syetrical covalent bond (%; O; >; + has no ola!it"2 bond shareselectrons A:A (diagra+

NAT REVIEWER BIOLOGICAL SCIENCE- Prepared by:JULEUS CESAR M. CADACIO, RN, RPT


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2. syetrical covalent bond results in one ato having

larger pull on electrons a'ing the electrons ore li'ely to

orbit the heavier eleent(s+ and less li'ely to orbit the

lighter eleent resulting in polarity: !C!!

electronegativity(see 1stdiagra on page ;+i. 4lectronegativity having a greater tendency to pull

electrons and thus partially charge or polari*e the covalently

bonded oleculeii. 4,: %;O O,ygen tends to pull electrons ore strongly so the

probability of shared electrons being in the O orbits is uch ore

li'ely and thus is electronegativeiii. Polarity the uneven distribution of charge causing areas of olecules to becoe

partially (D+ chargedE. Polar Bonding

1. Inter2olecular bonding 3 bonds beteen different olecules2. Intra2olecular bonding 3 bonds ithin the olecule itself (% & O bonds in %;O+3.

Polarity caused bonding 3 %ydrogen Bonding (%;O to %;O bonds+4. =arbon ill never for ionic bondsEall = bonds are covalent and can also bond to itself

and as such is the basis for biologyIII. Chemist!" of #ate!

A. Boiling 3 addition of enough energy to rip apart olecules hydrogen bonds1. 4ase of brea'ing bonds is dictated by the electronegative strength of the olecule2. Surface tension is another feature of the strength of the % bonds in ater

B. -ater nature is polar and thus it has attractive & repellent areas of charge1. .hese % bonds are responsible for the cheical & physical behavior results in fairly

strong bonds2. %as a high surface tension deonstrating strong cohesion because of these bonds3.

lso has a high latent heat of vapori*ation (hightheral capacity+

4. %;O good solvent for polar substances especially

ionically bound salts (hydrophilicsubstances+ as ater

brea's apart the polar ionic bonds! (see ig+5. Poor solvent for non2polar substances: a,es fats oils

etc! (hydrophobicsubstances+C. P% Scale easure of the acidity of a syste

1. %;O 3 %O%has a slight tendencty to turn into %00 O%2ions

i. In ionic for the hydrogen is a lone proton!ii. % ions are the basis of all acids

2. F%0G 3 12H$ and FO%2G 3 12H$ concentrations3. 3 2?og1of that nuber so:

i. 1A3 2AF%0G 3 12HF%0G 3 H% 3 H (also O% 3 H+4. .hus acid % is loer than H eaning an increase in %0concentration5. p% H 3 acidic p% H1J 3 basic6. 4,aple: %;SOJ: releases hydrogen into solution and thus is acidic driving p% don

i. >aO% siilarly donates O%2into solution reoving the %0concentration raising p%$. p% of a syste highly regulated%. Proton donors function as acid proton acceptors function as bases: thus %0 not

necessarily needed to be added to function as acid!I&.

Ca!'on Chemist!"A. =ovalent bonding only



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B. Shares four pairs of e2C. >aturally fors syetrical tetrahedron D. -ill bond to itself giving rise to variety of structures: ethane ethane

propane butane pentane he,ane septane octane nonane etc!1. =an also for ringed structures: =yclohe,ane ben*ene ring etc!2. 7ouble bonding 3 ending in 5ene6

E. Isoeris sae olecular forula but differing

arrangeents of atos1. Structural Isoers

i. =J%1 can be both butane or isobutaneii. =K%HO% can be propyl alcohol or isopropyl alcohol

2. Leoetric Isooers (cis/trans+ appear ith double bonds onlyi. .rans have Mu,taposed bonds hile cis isoers have bonds on the sae

side of the double bond3. Stereoisoers/4nantisoers irror iages of each other

i. Occurs hen there are J different structures around the =arbon atoF.

@unctional Lroups1. %ydro,yl Lroups O% group alcoholsi. %ydro,yl group becoes polar due to presence of O;and is thus very soluble in %;O!ii. O% group adds an 5ol6 ending: ethanol ethanol propanol butanol etc!

2. l'yl Lroup siple =2% based groups: ethyl ethyl al'yl etc!i. @orula is: =n%;n01

3. =arbonyl Lroup =%Oi. =ontains a double bonded o,ygen at the end of a olecule

(polar+ii. @ound in sugars aino acids nucleotidesiii. n aldehyde if at end of = bac'bone (2=%O+

i(. 'eytone if attached to interior of = bac'bone (N=O+4. =arbo,yl group =OO%

i. In aino acids fatty acids highly polar tends to release %0

functions as an acid5. ino group >%;

i. In aino acids and certain nucleotide basesii. -ater soluble acts as a ea' base (proton acceptor+ to becoe >%K

0(ioni*ed+6. Sulfhydryl group S%

i. In aino acid cysteine helps to stabili*e proteins (acting as disulphide bridge SS+$. Phosphate group POJ

2K

i. In nucleotides (.P+ 7> "> any proteins

phospholipids etc!ii. -ater soluble acidic

). Organic =oposition1. Polyer large olecule consisting of any siilar bonded saller units or onoers!

i. =onnection of onoers: condensation/dehydration reactions

a! 7ehydration/condensation reaction in hich to

olecules becoe covalently bonded to each

other through the loss of a sall olecule usually

%;Oii. 7isassebly of polyers: hydrolosis type of

cleavage reaction using ater to split a polyer attaching a hydro,yl group and a %



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ato derived fro a ater olecule to the e,posed site! 4ssentially the opposite of a

dehydration reaction!iii. 4n*yatic action assist in both hydrolysis and dehydration synthesis reactions

*. =arbohydrates consist of sugars and their polyers1. $onosaccharides the siplest sugars usually ith olecular forulas that are a

ultiple of =%;O (e,! Llucose ost coon onosaccharide =


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iii. %ead end of phospholipids is very polar phosphate group and thus hydrophilic3. Steroids (sterol2based lipids+ ex. Cholesterol

i. =oprised of = s'eleton of four interconnected rings (fig!+4. -a,es long chain fatty acids tightly pac'ed and bonded to long

chain alcohols or carbon rings! re alleable and hydrophilic!&. Proteins

A. ino acid an aino group (2>% K0+ a carbo,yl group (2=OO2+ the %0ato and one or

ore atos called it)s " group1. ino acids are the onoers that polyeri*e into protein polyers2. ;1 aino acids of huan biological concern3. Bonds beteen aino acids are peptide bonds ( =>= bonds li'e esters but using >+

i. 7ehydration synthesis/condensation reaction Moins the aino acidsii. Lrouping of ultiple aino acids is a ol"etide ,chain-iii. In peptide bond production there is alays a carbo,yl group (=OO%+ at one end and a

nitrogen (2>%;+ left over at the other = terinus & > terinusB. Structure

1.

.he sequence of aino acids in the polypeptide chain is the Priary Structure2. Secondary Structure is the regular % bonding in the chain resulting in either Q heli, or

pleated sheet3. .ertiary structure domainformation irregular bonding fro %ydrogen bonds disulfide

bridges (of the sulfhydryl group+ ionic bonding and hydrophobic interactions4. Ruaternary structure the final structure of the polypeptide chain hich deterines the

function of the protein!C. 7enaturation

1. ny change or disruption of the Jthprotein structure (change of heat p% etc+ disables the

protein fro doing its MobD. >ucleotides

1. ll nucleotides coprised of a sugar2phosphate bac'bone and one nitrogenous basei. .P contains three phosphate groups attached to its sugar!ii. Because the phosphate groups are very polar the release of those

bonds is e,treely e,egetic2. >ucleic cids

i. @ored by nucleotide onoers covalent bonds for beteen the sugar of one

nucleotide and the phosphate group of the ne,tii. 7>

a! ade up of J deo,yribonucleotide onoers (the nitrogenous bases are hat

differentiate the+ denine Luanine .hyine =ytosine

b! pentose (A = sugar+ bonded to nitrogenous base (L.=+ and to phosphate group

c! 7> contains the instructions for day to day operation and reproduction of thecell

d! Secondary structure of 7> fored by % bonding is hat fors the double

heli,iii. "> coposed of ribonucleotide onoers

a! Single stranded integral in protein synthesis

b! Substitute thyine base of 7> for uracil base

&I. Cell heo!"A. =ell functional unit of all living things the sallest unit ith the properties of life

1. ll have a region of 7> all have cytoplas all have plasa ebraneB. .ypes

1. Pro'aryotic priitive cells no ebranous fi,ed inner structure or nucleus



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ucleus contains the 7> of eu'aryotes directly

counicates ith the (rough+ 4"i. >ucleolis ass of proteins & copies of genes coding for

ribosoal ">3. >ucleoid region of cytoplas in pro'aryotes containing

7>4. 4ndoplasic "eticulu (4"+

i. Sooth 4" assists in the pac'aging and transport of aterials in the cellii. "ough 4" contains protein clups (ribosoes+ on ebrane all synthesi*es

lipids5. "ibosoes contained on all of rough 4" and in cytoplas assist in

.">S?.IO> of proteins6. $itochondria priary .P anufacturer of the cell (thus 5poerhouse6+ have their

on 7> and divide on their on$. Lolgi Body anufacture & pac'aging of inner & e,tra cellular aterials (proteins &

lipids+%. esicles ebrane bound grouping of cellular aterial act as cellular aterial

transportersi. ?ysosoes type/subset of vesicle that can open up and release digestive en*yes

brea'ing don cellsii.

Pero,isoes hold en*yes for digesting fatty acids aino acids and %;O;/. =hloroplasts (plant cell+ photosynthetic cell transfers sunlight & ater into .P10. =entral acuole (plant cell+ stores aino acids sugars ions and aste ta'es up A to

TU of the plant cell interior11. =ytos'eleton structurally supports gives shape to and oves eu'aryotic cell (not

present in pro'aryotes+i. $icrotubules largest s'eletal eleents regulates cell organelle placeent and

oveentii. $icrofilaents sallest s'eletal eleents reinforce cell shape reconfigure surface

etciii. Interediate filaents id si*ed eleents help reinforce the nucleus

&II. Bioloical Mem'!anesA. =oposed of Phospholipid Bilayer

1. One polar head to non2polar tails (heads hydrophilic tails hydrophobic+2. %ighly polar obMects cannot pass through bilayer because of hydrophobic tails3. ?arge olecules cannot pass through4. Lasses => pass through via 7iffusion O; ?iited aount of %;O sall non2polar

organicsB. .rans2ebrane proteins can e,tend though the ebranes

1. .ransporter ebranes are thus trans2ebrane proteinsi. Surface Proteins dhesion cceptor "ecognition =ounication .ransport

C. 7ynaic @luid $osaic .he lipid bi2layer in hich cople, structures ove (in constantotion thus dynaic+



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D. .ransport Proteins:1. Passive .ransport only driving force is natural olecular oveent (fro high to lo

concentration+!i. @acilitated 7iffusion protein hose Mob is to allo olecules through ebrane

fro high to lo concentrationii. quaporins specific transport proteins that allo %;O to passiii. Ion2selective channels ay be gated (controlled by cheical or voltage changes+i(. Las & %;O only diffuse no active puping(. Ososis 7iffusion of %;O across a sei2pereable ebrane

a! Osotic Pressure 3 .urger Pressure

b! .onicity concentration of solute2. ctive .ransport can ove olecules fro lo to high concentration but requires

energy to do soi. Priary active transporters get energy fro cleavage of .P pup olecules

against a concentration gradient via .P2ase activity alays have ; binding sites

one for .P other for transport of substrateii.

Secondary active transporters 5co2transporters6 use energy fro the gradient (e,!$itochondria+ as energy is released fro one gradient it is used to pup against

anotheriii. V=/ VW gradient difference in concentration/distance 3 the shorter the distance

needed to travel the faster the rate of diffusion3. Bul' .ransporters ll ebrane ediated

i. 4,ocytosis cell e,cretory functionii. 4ndocytosis inta'e of cellular aterial (ho aoebae feed+iii. Phagocytosis Solids ingestion of aterial by a cell for nutrition or distributioni(. Pinocytosis ?iquids droplets of liquid ingested by cell

&III. BioEne!etics t!ansfo!mation of ene!" in li(in thinsA.

4nergy the capacity for doing or'B. -or' e,ertion of a force through a distanceC. 1st la of .herodynaics 4nergy can neither be created or destroyed only

transferred/changed stateD. ;ndla of .herodynaics ll energy put into a syste cannot be e,tracted! >o syste

is 1U efficient (entropy+! ount of asted energy 3 efficiency of a systeE. Potential/Cinetic 4nergy

1. Potential: =heical $echanical Lradient 4lectrical every gradient has P4 (battery+2. Cinetic 4nergy C4 3 1/;$;

i. $olecular C4 theral energy a!'!a! %eat heat 3 9 of olecules , average C4 of

the olecules teperature is the easure of the average C4 of a syste3. 4nergy diagras =


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1. O,ygen @aily I loss of e2a'es o,ygen 5o,idi*ed6 (any loss of e 2 not necessarily

o,ygen+2. Lain of e23 reduced3. >7>7% 3 "educed >703 O,idi*ed

I. $etabolic pathays can be linear cyclical or branched+. "eversibility of reactions Z B

1. "eactions tend to flo in direction that releases lots of energyi. =oncentration 4quilibriu: Ceq3 FBG/FG

2. ?e=hatiler)s principle 5stressing a syste in equilibriu shifts the balance in the

opposite direction until equilibriu is established6i. 4,! 0 B Z = 0 7 (0 energy+

a! If: concentration of [ reaction speeds up concentration of B\=[ 7[. 4n*ye function only effect rate of reaction

1. Induced @it $odel: -arping of en*ye by substrate binding changes energy relationships

in the substrate thus loering activation energy changing of substrate into product(s+

after reaction causes attraction beteen en*ye/reactant to cease2.

\ teperature

\ activity (sloer olecules+3. [ teperature[ activity (until quaternary structure becoes denatured+4. p% free %0effects % bonds in tertiary or quaternary structure thus have a p% optiu

. =ontrol of 4n*ye ctivity1. llosteric ctivation/Inhibition Binding of a second olecule to a ;ndbinding site on

the en*ye increasing/decreasing en*ye activity2. =opetitive Interference/Inhibition process in hich

copetitor binds to active site on the en*ye and prevents

substrate fro being acted upon by en*ye3. @eedbac' Inhibition .he process by hich the products of a

reaction shut don the original reaction: i. llosteric can turn on & off en*yatic actionii. =opetitive can only a'e en*yatic action ore

difficultI. 4nergy "eleasing $echaniss

A. naerobic O;not required1. Llycolysis

i. lcoholic @erentation Xeast=O;0 4thanol (ethyl alcohol+ii. ?actate ferentation coplicated anialslactic acid forediii. 4,cretion of to,ins in anaerobic pathays

B. erobic respiration1.

Llucose as coon etabolite available frofoods converted fro other onosaccharides

cleaved fro disaccharides glycogen & starch2. =


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d! 4nergy associated ith the hydrogen carried on ; >7% carriers3. Preparatory steps to the Crebs =ycle (.= =itric cid =ycle+

i. .he to (K2carbon pyruvates+ are converted to to (;2carbon+ activated acetyl2

=oen*ye2 cople,esii. .his produces to =O;olecules as by2productiii. nd releases the energy of to >7% carriersi(. .his 5prepares6 the cetyl2=o for entry into

the Crebs cycle4. Crebs =ycle cyclic pathay that ta'es in the ;2

carbon cetyl =o and reoves its carbons

hydrogens and electronsi. Products are ;=O; K>7% @7%; and an

.P by substrate level phosphorylationii. =ycle

cran's

tice for

eachglucose

that

entersiii. .a'es

place in

the

itochondrial inner copartent5. O,idative (4lectron transfer+ Phosphorylation

occurs through action of transebrane en*yes in the cristal of the itochondria

8ses energy fro %0and their associated electrons brought by the carriers >7% and

@7%;i. =heiososis ability of certain

ebranes to use cheical energy to pup

hydrogen ions and then harness the energy

stored in the %0 gradient to drive cellular

or' (.P synthesis+ in this e,aple:

turns ;>7% & ; pyruvates fro

glycolysis into ;@7%;& ; cetyl2=oii. >7% & @7%; give up their electrons

hich poer %0 pups pushing the free

hydrogen outside the itochondrial atri,

this fors an electrical & concentrationgradient of %0 ions! .hese %0 ions flo

bac' through .P synthase poering 7P 0 Pi.Piii. O,ygen is the final e2acceptor ithout hich the entire process bac's up to the

pyruvate forcing the syste into anaerobic respiration as lactate (as pyruvate Z

lactase via ?7%+i(. 4nergy fro 1 >7% in CrebsK .P 1 @7%; 3 ; .P(. .hus in aerobic respiration: 1 olecule glucose 3 Llycolysis S?P! ; .P Crebs

S?P! ; .P 7% in Crebs 1Y .P ;>7% fro glycolysis J .P

;@7%;fro Crebs J .P ;>7% in pyruvate to cetyl =o stage < .P 3 K core2. 8sed radioactive isotopes of Sulfur (present only in the

protein coat+ and Phosphorus (only present in 7>+ to

deterine hether the genetic inforation as in the

protein the 7> or both!3. 7eterined it as the 7> hich carried the genetic

aterial!C. -atson =ric' et! l! (especially @ran'lin+

1. 7eterined through W2ray

crystalography and advanced

atheatical calculations that 7> is

shaped in a double heli,! (Strands are

antiparallel+



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2. 7ouble heli, consists of alternating phosphate2sugar

5rails6 ith nitrogenous base 5rungs6i. denine/Luanine Purines (double ringed bases+ii. =ytosine/.hyaine Pyridines (single ringed bases+iii. =/L ; %ydrogen bond attachent /. K % bond

attachent3. =hargaff)s "ules: States that /. L/= ust for 5rails6

in the double heli, the double rings are each atched

ith a single ring!II. 7> "eplication: (=hs 1K/1J+

A. $eselson & Stahl >o that 7> is 'non to be the

purveyor of genetic inforation being passed on ho is 7>

replicated#1. K $odels fro hich to chose conservative dispersive & sei2

conserv!2. Parent generation gron in heavy nitrogen (>1A+

hile subsequent "1 & "; generations gron inordinary nitrogen (>1J+3. "; Leneration then centrifuged to find out here the

7> ould end up telling the hich odel as

correct! (ll at the sae place for dispersive to distinct

places in "1 for conservative to distinct places in "; but not

"1 for sei2conservative+B. "ibose/7eo,yribose:

1. 7eo,yribose has only an % at the ;)= instead of an O%!2. "ibose has an O% on the ; =3. >otice: K) & A) =arbon attachent sites along hich replication

occurs:i. 4nd of 7> rail is the K) end sequence is K=2P2A=2P2K=2P2

A=2P2K=!!!

C. ctivity at replication (replication for' all ta'es place during S.L4 S of interphase+1. %elicase activity uninds the double2heli, prior to replication

(at the of the for'+2. =ople, en*ye 7> polyerase unraps 7> & begins

assebling along leading strandi. 7> polyerase is only able to build ne 7> in

direction fro K) to A) along the parent strand!

a! 7> polyerase releases to phosphates fro a freefloating nucleotide base!

b! 4nergy released by this drives the attachent of the

reaining P to an O% hanging off the K) = sugar of

the preceding 5rung6ii. .hus one strand can be replicated soothly (leading+ the

other strand cannot (lagging+3. 5chun'6 of "> Prier attaches along the ;ndparent (lagging+ strand

i. "> prier attaches to the lagging strand alloing 7> polyerase to build

5chun's6 of 7> along that strand!ii. .hese chun's being build fro "> prier by

7> polyerase are O'a*a'i fragents



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iii. O'a*a'i fragents sen together by 7> ligasei(. .he 7> contains an initiation and terination site alloing "> to 'no here

to start & stop4. fter this ligase 5seing6 action there are to strands of 7> coing out of the S phase

as sister chroatidsD. 7> "epair

1. =onducted by speciali*ed ligases and polyerases2. @ailure of these repair echaniss is thought to be a cause of aging

E. 8se of 7> inforation in the cell:1. =an only be done in L1& L;as 7> cannot control the functions of the cell hile it is

replecating or condensed into chroosoal for!2. 8se of the 7> aterial in the cell requires 5reading6 the language of 7> and

t!anslatinit into the language of protein structureIII. .ranscription/.ranslation

A. .ranscription the production of "> in nucleus! "> then leaves the nucleus

traveling to the ribosoes (in the rough 4"+ here .ranslation occurs!1. .ranslation the production of polypeptide chains at the ribosoes

B. =lasses of ">1. "> (essenger+ =arries the coding sequence to build a protein!2. r"> (ribosoal+ $aMor structural eleents of ribosoes! long ith proteins r">

olecules a'e up the ribosoes on hich protein synthesis occurs3. t"> (transfer+ Speciali*ed "> olecules that deliver specific aino acids to the

ribosoes for insertion into a groing polypeptide (protein+ in the sequence specified by

the ">4. ll transcribed fro 7> thus all produced in the nucleus

C. .ranscription Process Initiated at apromoter a base sequence on the 7> hich signals

the start of a gene1.

7iffers fro 7> replication in K ays:i. Only part of one 7> strand not the hole olecule is unound and used as the

teplateii. .he en*ye "> polyerase not 7> polyerase adds ribonucleotides one at a

tie to the end of a groing strand of ">iii. 8nli'e 7> replication transcription results in a single unbound strand of "> not

a % bonded double strand of 7>!2. Initiated at prooter"> polerase en*ye "> olecule copleentary to

the 7> base sequence3. "> ust go through a aturation process before serving as a teplate for protein

productioni. >on2coding portions of "> (int!ons+ are en*yatically 5snipped6 outii. tail and a cap are also attached to the "> that help it function at the ribosoe

D. .ranslation Process1. fter aturation "> travels along 4" to the ribosoe here it serves as a teplate

for protein anufacturei. !ansc!ition !oduces the m87A 9hose nucleotide 'ase se:uence tells the

!i'osome 9hat the aminoacid se:uence should 'e. he amino acid se:uence

dete!mines the (priary+ st!uctu!e of the !otein. ;!ima!" st!uctu!e of !otein

dete!mines :uate!na!" st!uctu!e of !otein< 9hich dete!mines function.2. >ucleotide base sequence on the "> is read three at a tie (triplet code or =O7O>+

i. Because there are J bases at each position and K positions in a codon there are J K3


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1J

a! 8L start codon 8 8L & 8L serve as stop codons

b! .hus )s

copleentary base sequence alloing attachent and

addition of aino acid 'non as >.I=O7O>+4. fter t"> attaches its aino acid it leaves the ribosoe

re2entering the cytoplas pool of aino2acids to reattach

the appropriate aino acid to its specific bonding site5. "ibosoe itself consists of to subunits (?arge & Sall+

i. .hese subunits of the ribosoe are assebled in the

nucleus and transported separately to the cytoplas

here they are assebled and attached along the

rough 4"E. K Stages of .ranscription1. Initiation 2 Initiator t"> binds to a sall ribosoal

subunit creating a sall subunit/t"> cople,i. t">/subunit cople, attaches to ">ii. .he start codon atches up ith the initiator t"> anticodoniii. .he large ribosoal subunit Moins and initiation coples

2. 4longation the ne,t t"> (after the previously entioned initiator t"> & ">

trans!+ ith its atching anticodon loads onto the second (56+ site of the ribosoe and

the "> transcript is advanced forard one codon in the ribosoe leaving the ost

recently attached t"> at the first attachent site (P+ and an open second attachent site

(+ on the ribosoei. >o the ne,t t"> ith its attached aino acid can lin' ith the "> transcript at

the 56 siteii. Peptide bond beteen the to aino acids at the P and sites is created elonatin

the polypeptideiii. .he process then repeats

3. .erination stage in hich a stop codon oves onto the platfor!i. Stop codon triggers the release of the protein and the "> fro the ribosoeii. "> can be used to generate another protein olecule or bro'en don to a'e

another "> transcriptI&. =hapter 11 Lenetics

A. $endel 8sing pea plants found indirect but observable evidence of ho parents transitgenes to offspring1. $endel as able to trac' the traits of his pea plants and as able to discern the patterns

shoing clearly observable patterns tracing the inheritance of traitsB. Basic Lenetics:

1. P13 Parent Leneration @13 first generation offspring @;3 ;ndgeneration offspring

2. $onohybrid cross 3 , aa 7ihybrid cross 3 BB & aabb 3 B , ab3. Lenotype genetic coposition Phenotype observed condition/coposition4. "h factor in huan blood (0 or 2+ signifying the presence of absence of the "h or 7

antigen in the blood! "h negative other having an "h 0 child can develop antibodies

against "h0 and eventually destroy those cells!5. =oplete doinance 3 "47 , hite 3 "47 Incoplete 3 "47 , hite 3 Pin' (because

of ultiple alleles coding for the sae trait+



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1A

&. Structural %eirarchyA. =ells.issuesOrgansOrgan SystesOrganisB. .as's of Physiology $aintenance of hoeostasis acquisition of O; & nutrients e,cretion

of aste protection fro attac'/inMury/disease reproductionC. .issues

1. 4pithelial e,posed to 5outside6 surface covering (s'in trachea etc+ can be glandular2. =onnective ?iving =ells in a non2living atri, that the living cells theselves secrete3. $uscle contractile tissue4. >erve "apid & specific counication

D. =ell ]unction .ypes1. .ight ]unctions Isolate deeper layers of a tissue fro the surface

i. ?ayers of protein fibers act to hold cells together a'e it difficult for obMects at

surface to or' their ay beteen the cells into deeper tissue layers (Lut trachea

bladder+2. dhering ]unctions Lreat physical strength holding cells together =ells held together

by protein plaque ($uscle s'in tendons etc+3.

Lap ]unctions rapid ion transfer beteen cells (allos for carrying of electrical signalthrough tissue + allo polar ions to pass through cell ebrane (heart+E. 4pitheliu

1. pical at top Basal at bottoEusually rests on a baseent ebrane hich 5glues6

epitheliu in place2. ll epitheliu is avascularEblood supply is in the baseent tissue3. Subclasses of 4pitheliu

i. ?ining/Surface Lut "espiratory tract

8rniary .ractii. Llandular ll e,ocrine glands seat acid

producers in stoach bile in liver etc

4. =ell Shapesi. Squaous (flat+ 7esigned to reduce friction

and often to be orn aay! Provides for a

large surface area and thus easily diffusesii. =uboidal ?arge internal volue often

have any itochondria and golgi bodies!

%igh producers & etabolically activeiii. =olunar have an apical and basal surface:

apical soeties has cilia on it large cellular

volue and are good secretory cellsi(. =ells ay be in a singler layer (siple+ or

stac'ed (stratified+F. =onnective .issue

1. ?arge variety of tissue types and levels of vascularityi. vascular (cartilage+ to highly vascular (bone+

2. ll characteri*ed by having living cells suspended in a non2living atri, hich the cells

theselves produce3. 7ense Irregular =onnective .issue: %uan S'in intestinal uscles etc atri, pac'ed

ith any fibroblasts and collagen fibers!4. 7ense "egular =onnective .issue: Orderly ros of fibroblasts beteen parallel tightly

pac'ed bundles of fibers! (.endons and ligaents+5. ?oose connective tissue (e,! 7og S'in+: @raeor' tissues for any organs and tissues

(atri, often sei2fluid+6. Speciali*ed =onnective .issues



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1eurons (>erve =ells+1. =ontain an input reigon and an output reigon!2. 7o not itose3. 4lectrically responsive: aintain a resting electrical gradient across the ebrane4. =onsists of: =ell body "eceptive area (dendrite+ and transission reigion usually a long

a,on!5. 4lectrical=heical4lectrical charges6. .ransduction at the synapse ensures one2ay transission perits integration

I. Ler ?ayer @ates1. 4ndoder ?ining of respiratory and digestive tracts (pancreas liver etc+2. $esoder S'eletal uscle outer covering of internal organs blood vessels & heart

notochord3. 4ctoder all

nervous tissue

epideris s'in and

hair epitheliu inner

ear retina of eye etc!

Started out ou outside

of 5blastula6 and igrated inard during developent+. %uan Organ Systes

1. Integuentary S'in and associated organs S'eletal $uscular >ervous 4ndocrine

Leneral cheical signaling =ardiovascular ?yphatic iuno2related & returns

fluids to blood strea "espiratory 7igestive 8rinary "eproductive. =avities of the %uan Body

1. Do!sal =ontains cranial & spinal cavities2. ho!acic =ontains pleural spaces (lungs+ and ediastinu (heart trachea esophagus

etc+3. A'dominoel(ic @ro the diaphra don (stoach liver intestines bladder etc+

. Planes/Positions of the Body1. nterior/Posterior front/bac'2. Superior/Inferior above/belo3. 7orsal/entral top/botto of J legged anial (fish+4. 7istal/Pro,ial far/close ith respect to body attachent (e,treities+5. $edial/?ateral close/far ith respect to the trun'6. .ransverse =ross2section at aist



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1H

$. @rontal Plane Shoulder to shoulder parallel to idth of body! (=oronal hen referring

to the head+%. Saggital Plane 7ivision into left and right sides along the syetrical a,is (id2

saggital+M. %oeostasis active aintenance of a constant internal environent7. @eedbac'

1. >egative @eedbac' ?oop Inverse relationship: fall in tep/p% 3 response 3 rise in ./p%i. =oponents: Sensor to deterine the controlled variable controller/integrator to

connect sensor to effector effector hich affects the controlled variableii. Set point the level that is aintained

2. Positive @eedbac' ?oop 7irect relationship: rise in tep/p% 3 response 3 further risei. 4,: =ontractions at childbirth nerve firing etc

3. >egative feedbac' loop allos for the aintence of stablity provided the disturbance is

not too large and overpoering for the functional response echaniss&I. >erve =ells =h! KJ

A. Structure:1.

Input *one: dendrites cell body2. =ouducting *one: ,on3. output *one: ,on endings (terinals+

B. .ransduction: .ransfer of signal fro one for to

another:1. =heicalelectrical=heical2. (input/trigger+(a,on+(output *one+

C. Ionic 7istribution across cell ebrane results in

ost cells carrying a slight negative charge1. >euron =ell $ebrane: selectively pereable depending upon charge/si*e etc!

i. 4ither active or passive channels (lea'age channels+

2. $ebrane potential the electrical charge generated by the slightly negative chargeinside the cell copared to the outside of the cell

3. change in voltage opens soe of the selective (active+ channels


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5566880 Biology Lecture Notes I