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Proteins
Introduction
Chapter24
Primary structure refers to the exact sequence of amino acids along a protein
chain
Secondary and tertiary structures refer to the further bending and folding of the
primary structure
Quaternary structure refers to the aggregation of more than one polyamide chain
All amino acids except glycine are chiral and have the L
configuration (as related to glyceraldhyde) at the carbon
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Amino acids
Structure and Names
Essential amino acids are not made by higher animals and must be
part of the diet
There are 8 essential amino acids for adult humans (see Table 24.1)
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Edman Degradation
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Structure
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Insulin
The structure of bovine insulin (shown below) was determined in 1953 by Sanger
Human insulin differs from bovine insulin at only three amino acids in its
sequence
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Proteins
Secondary Structure
These local conformations are specified in terms of regular folding patterns such
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Slight bond rotations are necessary between amide groups to avoid unfavorable
steric interactions between peptide side chains, leading to the pleated structure
The -pleated sheet is the predominant structure in silk fibroin
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The amide nitrogen has a hydrogen bond to an amino acid carbonyl oxygen that is
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Tertiary Structure
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Quaternary Structure
Hemoglobin
The subunits are shown in blue and green; subunits are shown in yellow and
cyan
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Introduction
The sides of the ladder are alternating sugar and phosphate units
The rungs of the ladder are hydrogen-bonded pairs of heterocyclic amine bases
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DNA is supercoiled and bundled into 23 chromosomes for packaging in the cell
nucleus
The set of all genetic information coded by the DNA in an organism is its genome
The set of all proteins encoded in the genome of an organism and expressed at
disease
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A nucleoside of DNA contains 2-deoxy-D-ribose and one of the following four bases
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Secondary Structure
Chargaff also noted that the ratio of A and T versus G and C varies
by species but the ratio is the same for different tissues in the
same organism
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Based on this data, Watson and Crick proposed the double helix
model of DNA (next slide)
Two nucleic acid chains are held together by hydrogen bonding between the
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Knowing the sequence of one chain allows one to also know the sequence of the
other
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Proteins have many critical functions, e.g., catalysis, structure, motion, cell
mRNA moves to the cytoplasm and the translation into proteins occurs using two
other forms of RNA: ribosomal RNA (rRNA) and transfer RNA (tRNA)
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Ribosomes - rRNA
A ribosome consists of approximately two thirds RNA and one third protein
A ribosome is a ribozyme ( an reaction catalyst made of ribonucleic acid)
The 30S subunit binds the mRNA that codes for the protein to be translated
The 50S subunit catalyzes formation of the amide bond in protein synthesis
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redundancy in the overall code and in the start and stop signals
N-formyl methionine (fMet) is the first amino acid incorporated into bacterial
protein and appears to be the start signal
fMet is removed from the protein chain before its synthesis is complete
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Translation
A tRNA with the anticodon for fMet associates with the fMet codon on the mRNA
A tRNA with anticodon UUU brings a lysine residue to the AAA mRNA codon
The 50S ribosome catalyzes amide bond formation between the fMET and lysine
The ribosome moves down the mRNA chain to the next codon (GUA)
A tRNA with the anticodon CAU brings a valine residue
The ribosome catalyzes amide bond formation between Lys and Val
The ribosome moves along the mRNA chain and the process continues, e.g., with
i.e. synthesized
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DNA molecules are replicated in such a way that a family of partial copies is
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afternoon
The Nobel Prize was awarded to K. Mullis in 1993 for invention of PCR
PCR requires:
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