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Frederick Griffith
• British bacteriologist
• 1928 = designed and performed experiment
on rats and bacteria that causes pneumonia.
• 2 strains of the bacteria
• Type S = causes severe pneumonia
• Type R = relatively harmless
Griffith’s Rats
1. First he injected living Type S bacteria into
rats:
• Second he injected dead Type S into the
rats.
• Next he injected living type R bacteria
• Finally he injected a mixture of living Type R
and dead Type S :
Results of experiments:
• Because the dead rat tissue showed living
Type S bacteria, something “brought the Type
S back to life”
• Actually one bacterial type incorporated the
DNA, or instructions, from the dead bacteria
into its own DNA
• Known as transformation. Confirmed by
Avery, MacLeod, and McCarty in 1944
Oswald Avery
• Canadian
biologist (18771955)
• Discovered
DNA in 1944
with a team of
scientists.
Hershey and Chase
• 1952
• Attempted to solve
the debate on
whether DNA or
proteins are
responsible for
providing the
genetic material.
• They used a
bacteriophage (a
virus which
attacks bacteria)
to prove that
DNA was
definitely the
genetic material.
Phoebus A. Levene
• Russian born; immigrated to America,
moves to Europe.
• 1920’s discovered nucleotides (building
blocks of DNA)
1. Sugar
2. Phosphate group
3. Nitrogenous base
Composition of DNA
Components and structure of DNA
• A very long molecule. 4 nitrogenous bases:
Chargaff’s rules
• The relative amounts of adenine and thymine
are the same in DNA
• The relative amounts of cytosine and guanine
are the same.
• Named after Erwin Chargaff
Rosalind Franklin

• Used X-Ray diffraction to
get information about the
structure of DNA:
Structure of DNA
• Discovered in 1953
by two scientists:
• James Watson
(USA)
• Francis Crick (GBR)
• Known as the
double-helix
model.
The double-helix
• A twisted ladder with two long chains of
alternating phosphates and sugars. The
nitrogenous bases act as the “rungs”
joining the two strands.
How long is the DNA molecule?
Chromosomes & DNA replication
• The nucleus of one human cell contains
approximately 1 meter of DNA.
• Histones = DNA tightly wrapped around a
protein
• Nucleosome:
Chromosome structure:
DNA replication

• Must occur
before a cell
divides.
• Each new cell
needs a copy of
the information
in order to grow.
DNA replication. Why needed?
• Before DNA strand can
be replicated or
copied it must be
“unzipped”
• DNA polymerase
(enzyme that unzips)
• Starts at many
different points. Why?
Completing the replication
• After the DNA
molecule comes
apart, bases of
free nucleotides
in the nucleus
join their
complimentary
bases.
RNA
• Very similar to DNA.
• Exceptions:
1) Ribose is the 5-carbon sugar
2) Uracil replaces thymine
3) Single-stranded
mRNA (messenger)
• Copies genetic
code of DNA by
matching bases.
• Occurs in the
nucleus.
• DNA changing to
RNA
TRANSCRIPTION
• DNA is copied into mRNA with the
aid of RNA polymerase.
• The RNA polymerase will bind to
promoters that act as signals in the
DNA sequence to make RNA.
Transcription continued:
Exons and Introns
• EXONS
• A segment of DNA in
eukaryotic organisms
that codes for a specific
amino acid

• INTRONS
• A segment of DNA that
does NOT code for an
amino acid.
Confusing genetic terms:
• Polypeptide = a chain of amino acids.
• Protein = a complex structure composed of
polypeptides
• Amino acids = smallest structural unit of a
polypeptide.
• Gene = a distinct unit of material found on a
chromosome
Reading the genetic code
• The genetic code is responsible for
building all the proteins in the body using
20 different amino acids.
• How many 3 letter words can you make
from the letters A,T,G and C?
• Answer: 64
Codons
• A three letter “word” that specifies
an amino acid.
Genetic code:
tRNA (transfer)
• approx. 80 nucleotides in
length.
• Cross-like shape
• At one end an amino acid
is attached
• At the other end there is
an anticodon
• Acts like a truck
Polypeptide assembly
• Translation = reading
or “translating” the
RNA code to form a
chain of amino acids.
• Known as protein
synthesis
• Occurs in the
cytoplasm. (p.304)
Mutations
• The source of variation in a genetic
sequence.
• Can be either gene or chromosomal
mutations.
• Point mutations = a change in a single
nucleotide in a sequence of DNA.
Frameshift Mutation
• Inserting an extra nucleotide which, in turn,
shifts the entire sequence one way or the
other.
Chromosomal mutations
• Involves a change in the number or structure
of the chromosomes.
• Deletion : when a piece of a chromosome
breaks off and is lost.
• Duplication : when a segment of a
chromosome is repeated
• Inversion : when a segment of a chromosome
is reversed.
More chromosomal mutations
• Translocation :
when part of a
chromosome
breaks off and is
attached to a
non-homologous
chromosome.
Control of gene expression
• Genes are often like light switches
that can be turned off and on.
• Operon = occur in prokaryotes.
(bacteria) different genes that work
together to activate gene functions
Eukaryotic gene expression

• Controlled by
complex
sequences of
DNA.
• Example:
“TATA box”
Protein Structure
• Serve various function including structural roles,
catalysts, transporter and hormones
• Polymers of amino acids covalently linked
through peptide bonds into a chain
• Each of amino acid has a fundamental design
composed of a central carbon bonded to ;
i. a hydrogen
ii. a carboxyl group
iii. An amino group
iv. A unique side chain of R-group
• the characteristic that distinguishes one amino
acid from another is its unique side chain, and
it is the side chain that dictates an amino acids
chemical properties
• The unique side chains confer unique chemical
properties on amino acids, and dictate how
each amino acid interacts with the others in a
protein.
Peptide bonds are formed between the carboxyl
group of one amino acid and the amino acid of the
next amino acid

 Peptide bond formation occurs in a condensation reaction
involving loss of a molecule of water
 The head-to-tail arrangment of amino acids in a protein means
that there is a amino group on one end (called the aminoterminus or N-terminus) and a carboxyl group on the other end
(carboxyl-terminus or C-terminus).
 The carboxy-terminal amino acid corresponds to the last one
added to the chain during translation of the messenger RNA.
Levels of Protein Structure
• Structural features of proteins are usually described at
four levels of complexity
a. Primary structure
b. Secondary Structure
c. Tertiary Structure
d. Quaternary Structure
Primary Structure
• - the linear arrangement of amino acids in a
protein and the location of covalent linkages
such as disulfide bonds between amino acids
Secondary Structure
• areas of folding or coiling within a protein;
examples include alpha helices and pleated
sheets, which are stabilized by hydrogen
bonding
Tertiary Structure
• the final three-dimensional structure of a
protein, which results from a large number of
non-covalent interactions between amino
acids.
Quaternary Structure
• Two or more tertiary proteins joined
• non-covalent interactions that bind
multiple polypeptides into a single, larger
protein. Hemoglobin has quaternary
structure due to association of two alpha
globin and two beta globin polyproteins.

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Dna, rna, protein

  • 1. sdn
  • 2. Frederick Griffith • British bacteriologist • 1928 = designed and performed experiment on rats and bacteria that causes pneumonia. • 2 strains of the bacteria • Type S = causes severe pneumonia • Type R = relatively harmless
  • 3. Griffith’s Rats 1. First he injected living Type S bacteria into rats:
  • 4. • Second he injected dead Type S into the rats.
  • 5. • Next he injected living type R bacteria
  • 6. • Finally he injected a mixture of living Type R and dead Type S :
  • 7. Results of experiments: • Because the dead rat tissue showed living Type S bacteria, something “brought the Type S back to life” • Actually one bacterial type incorporated the DNA, or instructions, from the dead bacteria into its own DNA • Known as transformation. Confirmed by Avery, MacLeod, and McCarty in 1944
  • 8. Oswald Avery • Canadian biologist (18771955) • Discovered DNA in 1944 with a team of scientists.
  • 9. Hershey and Chase • 1952 • Attempted to solve the debate on whether DNA or proteins are responsible for providing the genetic material.
  • 10. • They used a bacteriophage (a virus which attacks bacteria) to prove that DNA was definitely the genetic material.
  • 11.
  • 12. Phoebus A. Levene • Russian born; immigrated to America, moves to Europe. • 1920’s discovered nucleotides (building blocks of DNA) 1. Sugar 2. Phosphate group 3. Nitrogenous base
  • 14. Components and structure of DNA • A very long molecule. 4 nitrogenous bases:
  • 15. Chargaff’s rules • The relative amounts of adenine and thymine are the same in DNA • The relative amounts of cytosine and guanine are the same. • Named after Erwin Chargaff
  • 16. Rosalind Franklin • Used X-Ray diffraction to get information about the structure of DNA:
  • 17. Structure of DNA • Discovered in 1953 by two scientists: • James Watson (USA) • Francis Crick (GBR) • Known as the double-helix model.
  • 18.
  • 19. The double-helix • A twisted ladder with two long chains of alternating phosphates and sugars. The nitrogenous bases act as the “rungs” joining the two strands.
  • 20. How long is the DNA molecule?
  • 21. Chromosomes & DNA replication • The nucleus of one human cell contains approximately 1 meter of DNA. • Histones = DNA tightly wrapped around a protein • Nucleosome:
  • 23. DNA replication • Must occur before a cell divides. • Each new cell needs a copy of the information in order to grow.
  • 24. DNA replication. Why needed? • Before DNA strand can be replicated or copied it must be “unzipped” • DNA polymerase (enzyme that unzips) • Starts at many different points. Why?
  • 25. Completing the replication • After the DNA molecule comes apart, bases of free nucleotides in the nucleus join their complimentary bases.
  • 26. RNA • Very similar to DNA. • Exceptions: 1) Ribose is the 5-carbon sugar 2) Uracil replaces thymine 3) Single-stranded
  • 27. mRNA (messenger) • Copies genetic code of DNA by matching bases. • Occurs in the nucleus. • DNA changing to RNA
  • 28. TRANSCRIPTION • DNA is copied into mRNA with the aid of RNA polymerase. • The RNA polymerase will bind to promoters that act as signals in the DNA sequence to make RNA.
  • 30. Exons and Introns • EXONS • A segment of DNA in eukaryotic organisms that codes for a specific amino acid • INTRONS • A segment of DNA that does NOT code for an amino acid.
  • 31. Confusing genetic terms: • Polypeptide = a chain of amino acids. • Protein = a complex structure composed of polypeptides • Amino acids = smallest structural unit of a polypeptide. • Gene = a distinct unit of material found on a chromosome
  • 32. Reading the genetic code • The genetic code is responsible for building all the proteins in the body using 20 different amino acids. • How many 3 letter words can you make from the letters A,T,G and C? • Answer: 64
  • 33. Codons • A three letter “word” that specifies an amino acid.
  • 35. tRNA (transfer) • approx. 80 nucleotides in length. • Cross-like shape • At one end an amino acid is attached • At the other end there is an anticodon • Acts like a truck
  • 36. Polypeptide assembly • Translation = reading or “translating” the RNA code to form a chain of amino acids. • Known as protein synthesis • Occurs in the cytoplasm. (p.304)
  • 37. Mutations • The source of variation in a genetic sequence. • Can be either gene or chromosomal mutations. • Point mutations = a change in a single nucleotide in a sequence of DNA.
  • 38. Frameshift Mutation • Inserting an extra nucleotide which, in turn, shifts the entire sequence one way or the other.
  • 39. Chromosomal mutations • Involves a change in the number or structure of the chromosomes. • Deletion : when a piece of a chromosome breaks off and is lost. • Duplication : when a segment of a chromosome is repeated • Inversion : when a segment of a chromosome is reversed.
  • 40. More chromosomal mutations • Translocation : when part of a chromosome breaks off and is attached to a non-homologous chromosome.
  • 41. Control of gene expression • Genes are often like light switches that can be turned off and on. • Operon = occur in prokaryotes. (bacteria) different genes that work together to activate gene functions
  • 42. Eukaryotic gene expression • Controlled by complex sequences of DNA. • Example: “TATA box”
  • 43. Protein Structure • Serve various function including structural roles, catalysts, transporter and hormones • Polymers of amino acids covalently linked through peptide bonds into a chain • Each of amino acid has a fundamental design composed of a central carbon bonded to ; i. a hydrogen ii. a carboxyl group iii. An amino group iv. A unique side chain of R-group
  • 44.
  • 45. • the characteristic that distinguishes one amino acid from another is its unique side chain, and it is the side chain that dictates an amino acids chemical properties • The unique side chains confer unique chemical properties on amino acids, and dictate how each amino acid interacts with the others in a protein.
  • 46. Peptide bonds are formed between the carboxyl group of one amino acid and the amino acid of the next amino acid  Peptide bond formation occurs in a condensation reaction involving loss of a molecule of water  The head-to-tail arrangment of amino acids in a protein means that there is a amino group on one end (called the aminoterminus or N-terminus) and a carboxyl group on the other end (carboxyl-terminus or C-terminus).  The carboxy-terminal amino acid corresponds to the last one added to the chain during translation of the messenger RNA.
  • 47. Levels of Protein Structure • Structural features of proteins are usually described at four levels of complexity a. Primary structure b. Secondary Structure c. Tertiary Structure d. Quaternary Structure
  • 48. Primary Structure • - the linear arrangement of amino acids in a protein and the location of covalent linkages such as disulfide bonds between amino acids
  • 49. Secondary Structure • areas of folding or coiling within a protein; examples include alpha helices and pleated sheets, which are stabilized by hydrogen bonding
  • 50. Tertiary Structure • the final three-dimensional structure of a protein, which results from a large number of non-covalent interactions between amino acids.
  • 51. Quaternary Structure • Two or more tertiary proteins joined • non-covalent interactions that bind multiple polypeptides into a single, larger protein. Hemoglobin has quaternary structure due to association of two alpha globin and two beta globin polyproteins.