Genetic Code

Front 1

compare DNA vs Protein
-length
-amt of info
-ability to replicate
-size of str.
-stability to make str.
-organization
-how to deal with info

Back 1

-very long (millions)/comparitively short (100s)
-lots of info/less info
-can replicate/cannot rep
- thin and fragile/ thick globule
-less stable to make str./more stable to make
-not self org/ self org

Front 2

what is the lang of nucleic acids ? its purpose

Back 2

-the lang of nucleic acids is the linear seq of the NT bases
- the purpose of the lang is to be translated into polypeptides (proteins)

Front 3

what are codons

Back 3

- triplets of bases that specify all amino acids

Front 4

what processes are localized in the nucleus / cytoplasm

Back 4

- replication and transcription
- translation occurs in the cytoplasm

Front 5

what two stages does DNA specify the syn of proteins

Back 5

transcription and translation

Front 6

discuss the life functions proteins

- structural
- dynamic
- contractile
-transport
- storage

Back 6

- structural- make cells and organelles
- dynamics- catalyze rxn/enyzmes
-contractile- muscle and cytoskeleton
- transport - red blood cells
- storage - in seeds

Front 7

who was the first to propose a relationship between genes and protein productions? what was studied

Back 7

- archibald garrod
- studied patients who had defects in their ability to metabolize certain compounds

Front 8

waht was garrod particularly interested in ? how was it characterized?

Back 8

-he was interested in alkptonuria- occurs when the body accumulates abnormal levels of homogentistic acid
- characterized by black urine, skin and cartilage

Front 9

FIndings of Garrod exp

Back 9

- alkaptonuria was due to missing enzyme -homogentisic acid oxidase
-follow a reccessive pattern of inheritance
- disease is an inbro error of metabolism

Front 10

in the 1940, who where the two individuals that displayed interest in the relationship between the genes, enzymes, and traits

Back 10

George Beadle and Edward Tatum

Front 11

What was beadle and tatum's genetic model; # of trains and what type

Back 11

neurospora crassa - common bread mold
- more than 2000, each were irridated to produce mutation

Front 12

Findings
name the vitamins

Back 12

-three strains were found without the ability to grow- growth was restored only after a vitamin was added
-vitamins : 1-3 ; pyridoxine, thaimine, and p-aminobenzoic acid

Front 13

How were the normal strain in the beadle and tatum exp syn
- discuss what was found of the mutant strains

Back 13

vitamins were synthesized by cellular enzymes
- in mutant strains, it was found that a genetic defect prevented the syn of the protein needed to produce the vitamin

Front 14

beadle and tatum conclusion

Back 14

a single gene controlled the syn of a single enzyme
-one gene-one enzyme theory

Front 15

how is the beadle and tatum theory later modified

-what does polypeptide and protein denote

Back 15

- enzymes are only on category of proteins
- some proteind are composed of two or more different polypeptides
- polypeptide denote structure
- protein- denote function

Front 16

identify terms
-marco
-monomer
-polymer
-condensation
-hydroylsis

Back 16

-monomer; mono= one, mer=part -- basic or single part
-polymer; poly=many; long molecule that is made up of many part
-condensation- a rxn that synthesizes the addition of parts
-hydrolysis- occur by degradation and digestion to subtract parts

Front 17

discuss fundamental triad and hierarhies

Back 17

-subsystems join to make system join to make super systems
-subsubunits join to make subunits which aggregate to make units

Front 18

discuss the three basic structures that make up an amino acid (aa)

Back 18

- the monomer of a protein polymer is an amino acid
- basic structure consist
1) start with an amino group
2) end with a carboxyl group
3) have a middle carbon
4) the middle carbon can have one of the 20 different side chainds- each different side chain makes for a difft aa

Front 19

how many possible proteins are known to be on the planet earth

Back 19

-20^length of protein

Front 20

what are the four levels of the structures in protein

Back 20

primary, secondary, tertiary and quaternary

Front 21

primary
secondary
tertiary
quaternary
pentary

Back 21

-is it amino acid seq
-local shape
-total shape
-a protein joined with other proteins
- joined together complex

Front 22

protein primary structure

Back 22

- may range from 250-300 aa long (polypeptides)
- at first forms random coils which change due to the binding of h -bonds with other aa - creates two types of next level structure

Front 23

what dictates the progression from primary to 3d structure

Back 23

- the aa seq within the polypeptide chain

Front 24

how do proteins make a link together

Back 24

- the amino acids line up from tail to head - carboxtl grp is near the amino group of the next aa-- enzyme peptidyl transferase -causes the condensation rxn , a dehydration type which releases water made from side chain of the tail and head
-a new covalent bond of two aa makes a dipeptide
- more additions make tri, tetra, oligo- peptides

Front 25

why is the primary structure strictly controlled

Back 25

-the coding for the seq is crucial- changes to key aa sites may lead to genetic diseases
- an example is sickle cell amenia which occur due to one change in the alpha chain

Front 26

protein secondary structure

Back 26

-alpha helices and beta ribbons
- alpha helices- 3.5 aa downstream
-beta ribbons- have aa's a longer distance away; make two parts line up next to each other
-can be parallel and anti parallel
-

Front 27

protein tertiary structure

Back 27

-disulfide bonds or ionic assoc due to left over aa charges - results in random coil with mixed in secondary struct. that fold into 3D struct
- 3D struct. depends on aa sequence

Front 28

hydrophobic
hydrophilic

Back 28

-hate water- fold inside
-love water- face surface

Front 29

quaternary struct

Back 29

-some functions require two or more proteins
- 4th level struct. change over time

Front 30

denaturation

Back 30

- occurs when structure changes and function cannot occur

Front 31

nonpolar and charger aa are

Back 31

hydrophilic

Front 32

what are two types of secondary structures; how are they stabilized

Back 32

-alpha helix
-beta sheet
-stabilized by h bonds

Front 33

tertiary structures

Back 33

-still composed of one polypeptide-- made up of short regions of secondary structure
- 3D

Front 34

quaternary

Back 34

-made up of two or more polypeptides
-form when polypeptides combine to make a functional protein

Front 35

what relies on the Genetic code

Back 35

- the NT lang of mRNA is translated into the amino acid language of proteins