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Bio 118
Exam 3
| Question | Answer |
|---|---|
| Building Blocks of Life | H C N O |
| H C N O make up what perent of all material in organisms | 96% |
| Covalent Bond | Unpaired e- are shared by each atom to fill their orbitals-very strong |
| Non polar covalent bond | electrons are evenly shared bt 2 atoms |
| polar covalent bond | one atom hols shared e- more thn other- assymetrically shared |
| hydrogen bonds | bt h20 and other polar molevules or ions |
| ionic bond | electrons are completely transfered form one atom to the other |
| cation | pos charge -loose ee- |
| anion | neg chage- gain e- |
| Water | Life originated and based in/on water great solvent |
| why is water a great solvent | h-o bonds in h20=polar covalent, partial + can react with partial - and can bond w/in it |
| acid base reac and pH | proton doner-acid transfers proton to proton acceptor-base |
| endothermic | reax absorb heat to proceed, heat h20 ex.boiling into steam |
| exothermic | reac release heat ex. explosion |
| what is energy | the ability to work or supply heat |
| types of energy | potential->stored energy kinetic->energy of movement thermal->measured as temperature |
| First law of thermadynamics | energy is conserves, not created.not destroyed, can be transgerred or transformed |
| molecules contain stored energy | sugar molecule- high potential energy=>more order carbon dioxide(almost lowest) and h20-lower potential energy=> less order |
| temperature and concentration in chemical reaxtions cause... | more reactant collisions and faster reaction rates |
| Breaking carbon-hydrogen bonds... | releases energy |
| to form carbon hydrogen bonds | energy must be added |
| Importance of Carbon | 4 unpaired e-; can make 4 covalent bonds almost all molcules found in organisms contain a c-c bond; called organic molecule |
| carbon with funcitonal group contains | contain H, N or O atoms bonded to carbon; gives organic compounds it specific behavior |
| Amino | Attract Proton |
| Carbonyl | linmk molecules into larger co mpounds |
| Carboxyl | releases a proton |
| hydroxyl | act as weak acids |
| phosphates | have 2 neg charges |
| sulfhydryl | link to others by disulfide bonds |
| amino acid structure | all proteins are made form just 20 amino acid subunits all have: central C atom, H2N(amino functional group), COOH (carboxyl functional group), H(hydrogen atom), and a variable side chain(R) |
| Amino Acids Become Easily | Ionized |
| Amino Group | atracts a proton,, becomes a base so, in H2O-> amino and carboxyl group ionize to NH3+ Coo- helps amino acids stay in solution and makes them more reactive |
| Amino Acid Side Chain | the 20 amino acids differ only in variable side chain, R-Groups, attached to central atom |
| R-groups differ in | size, shape, reactivity, interactions wih water(key to protein reaction) |
| R-Groups can be | non polar(not why will raec with H2O polar electrically charge(react w/ H2O very well) |
| Non Polar Amino Acids | Side chains have no charge do not form hydrogen bonds with H2O hydrophobic-> tend to group together to avoid water |
| Polar Amino Acids | chains can be polarized to give partial - or + carge can form hydrogen bonds with water hydrophillic |
| Electrically charged amino acids | r side chains can be ionized to become acidic or basic can form ydrogen bonds with water hydrophillic |
| amino acid side chain chem reactivity | those with mostly C and H rarely chemically reactive, behavior depends on r-group (size and shape) those with OH, NH2, COOH, or S are more chemically reactive |
| Isomers and types | molecules with same molecular formula but different structures structural, geometric and optical |
| structural isomers | same atoms but diff. order in which covalant bonds attach |
| geometric isomers | same atoms but diff. arrangement of the atoms or groups on eitehr side of a double bond or ring structure(chain or ring structure) |
| optical isomers | same atoms but diff. arrangement of atoms or groups around a carbon atom that has 4 diff. groups attached (mirror image) |
| Macromolecules | Large molecules made up of smaller molecules joined together ( polymers) |
| Monomers polymerize into | polymers |
| monomers | small building blocks amino acids, sugars, nucleotides |
| polyers | long molecules composed of small repeating subunits proteins, polysacchrisdes, nucleic acids(DNA RNA) |
| Amino Acids polymerize to form | proteins |
| polymerization | process of linking monomers to form polymers requires energy and is not spontaneous |
| how are polymers made | monomers polymerize through condensation reactions a water molecule gain monomer monomers are removed from polymers by hydrolysis; releases a monomer |
| The Peptide Bond | condensation reaction bonds -carboxyl group of one amino aid to the amino group of another to form a peptide bond. NOT THE R GROUP |
| Linking several amino acids together forms | polypeptide |
| individual amino acids | residues |
| A polypeptide | Flexible has directionality: N-terminus has a free amino group, C- Terminus has a free carboxyl group side chains extend out from the backbone R-Group conform the enzymes |
| Oligo Peptides (or just peptides) | less than 50 amino acids |
| Proteins | More than 50 amino acids |
| Proteins Structures | 4 levels of stucture Primary secondary tertiary quaaternary |
| Primary Structure | Its unique sequencce of amino acids every protein has a unique seq. of amino acids there are 20^n dif polypeptides of a length of "n" |
| Different amino acids affect protein shape- how | the amino r-group of a protein effect sie shape chemical activity and reactions with water just a single amino acid change can radically change the proteins function |
| Secondary Structure | results from hydrogen bonding between carboxl oxygen of one amino acid to amino hydrogen of another residue (folds so dif parts can interact) hydrogen bonds are bt atoms in backbone-not the side chain polypeptide must bend to allow this hydrogen bonding |
| Shape of secondar structure | forms an alpha-helix- backbone is coiles or beta pleated sheat, backbone bends at angles a proteins 2nd structure increase stability |
| Tertiary structure | polypeptide 3D shape bue to RGroup causes polypeptide to bend and fold into precise shape |
| interactions in third structure | hydrogen bond-bt rsidechaind and COOH, bt 2 r ionic -bt ionized amino and COOH rside vanderwaals interactions-weak hydrophobic interactions, nonpolar amino acids interact to avoid polar water covalent disulide- bt 2 sulfur atoms of cysteine amino acids |
| primary , secondary, and tertiary structures | are reactions within an individual peptide: quaternary is between two ro more |
| quaternary structure | interaction of 2 or more proteins subunits |
| how to proteins fold properly | some fold naturally-ribonuclease others need help to fold correctly |
| denatured proteins | an unfolded protein... unable to function normally |
| molecular chaperones | proteins that interact and help other proteins fold correctly in cells |
| what do proteins do | antibodies motor and contractile proteins for movement hormones and receptors structure transport molescules into and out of the cell enzyme |
| catalyst | substance that increases the rate of a chem reax. without itself undergoing any permenent chemical change lowers activation energy of reaction does not chaing free energy not consumed in reation |
| enzymes | protein catalysts speed up and control biological reactions most bio chem rex only occur in presence of enzyme |
| How do enzymes work | bring substrates together in spec. position that faciliate reax (very specific (only in one reax) substrates bind to enzyme active sit interactions bt enzyme and substrate: stabalize transition stae and decrease activation energy |
| Induced Fit | a conformational or shape change of an enzyme when the substrate binds to the active site |
| Enzymes active site | active site rgroups interact w. substrate : Hbonging, temp. covalent bonding durign transfer os atoms, protom transefer through acidic or basic rgroups |
| enzyme action 3 steps | initiation, transistion state facilitation, termination |
| initiation | reactants bing to active site in specific orientation -specific orientation enhances interactions |
| transition state facilitation | enzyme changes shape substrate binding induces formation of transition site interactions bt enzyme and substrate lower activation energy req. for the reax |
| termination | the resulting reax products -low affinity for active site (dont fit) -released from enzyme -enzyme is unchanged after reax |
| Do enzymes act alone | some act alone, some require cogfactors to function or coenzymes usually in active site, involved in transition state stabilization |
| enzyme regulation | competitive inhibition -molecule similar in size and sape to substrate. conpetes with substrate for active site bonding |
| enzyme kinetics | speed/rate of enzyme action -products produces/sex 1-@low substrate conc. rate product forms increased linearly for a given increase in substrate conc. 2-@high substrate conc. rate of product form levels out |
| effects of temperature on enzyme function | affects movement too high-denature too slow- slows done enzyme reax and energy of substrate enzymes function best @ particular functions... works best @ about 40 C (human body temp 36 C) |
| effects of pH on enzyme function | affects charge of rside chaines (caboxyl and amino groups no low if it normally is high, carchge will mean enzyme wont work. |
| What are Nucleic Acids | polymer of nucleotides-ribonucleic acid (RNA) and Deozyribonucleic Acids( DNA) |
| Nucleotide | basic component of nucleic acids phosphate group sugar (5 C ring structure) #ed clockwide |
| two types of sugars | Ribose in Ribonucleotides and hydrocyl(OH) group on #2 carbon Deoxyribose in DNA be able to energyze |
| Purines | Adenin and Guanine 2 rings found in DNA and RNA |
| Pyrimidines | cystosine, uracil and thymine- one ring RNA contains cytosine and uracil.. DNNA contains cystosine and thymin |
| Nucleotide polymers form/nucleictides polymerize to produce | nucleic acids |
| Nucleotides polymerize through | condensation reax(rid water) nucleotide monomers joined by phosphodiester linkade bt OH on 3'C of one nucleotide and phosphate group on 5' C of another |
| Polymers of RNA | the sugar phosphates create the backbone -has a direction(read from 5' to 3') made from ribonucleotides |
| how to nucleotides polymerize into nucleic acids | activated nucleotides-free energy raised- energize by adding two extra phosphate groups/nucleotide phosphorylates nucleotides provide energy for polymerization reax (similar to ATP) |
| DNA | two antiparallel DNA strange hydrophilic sugar-phosphate backbone facing exterior -neg charged phosphates on outside puring-pyrimidine pairs on interior (packer close together) |
| Base Pairing | two dna strands have complimentary bp's G-C->3 hyrogen bonds A-T->weaker pair-2 Hbonds #purines=#pyrimidines double helix (primary structure is seq. of base, sec. struct. is 2 antiparallel strands) |
| Information containing molecule | provides mechanism for DNA replication each strand serves as a template for a new complimentary strand forms template for its own synthessis |
| DNA synthesis | break the hbonds bt bp's DNA can seperate each strande serve as template for new strand results in 2 strands provide for 2 new dna strands exact copies |
| RNA | prim. struc. similar to DNA but Uracil instead of Thymine ribose instead of Deozyribose (O group on ribose makes RNA more reactive and less stable than DNA) sensitice to pH temp and reactive chem. |
| Primary structure of RNA | nitrogeneous base sequence (5'-3') |
| Secondary structure of RNA | due to complimentary AU and GC bp's can form hbonds w/ complimentary bases onsame strand bases bind compluimentary bases and form antiparallel RNA segment hairpins form spontaneously (hairpins and other RNA 2 structures can have more folds) |
| Generalized chemical formula for Carbohydrates | (CH2O)n contain carbonyl group (C=O) several hydrocyl func. groups (OH) many C-H bonds |
Created by:
shirixo
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