Insulin: Weight = 5733, 51 amino acids Glutamine Synthetase: Weight = 600,000, 468 amino acids
Amino Acids & Dehydration Synthesis Amino acid structure: Functional groups Peptide bonds
Sample amino acid structures: carboxyl group-bluealpha carbon-gray amino group-greenR groups-beige
The twenty essential amino acids. Note R groups in blue
Amino Acids w/ various R groups
Nonpolar amino acids
Neutral Amino Acids
Ionic amino acids
Amino acids are joined together in proteins by peptide bonds. A peptide bond forms between the carboxyl group of one amino acid (amino acid 1 in the figure preceding) and the amino group of the adjacent amino acid (amino acid 2).
Dehydration synthesis
Dehydration synthesis animation
Dehydration Synthesis
Dehydration Synthesis : Amino acid 1 Amino acid 2 Dipeptide (Peptide bond) Amino group
Protein Structure Amino acid structure Dehydration synthesis
Insulin: Weight = 5733, 51 amino acids Glutamine Synthetase: Weight = 600,000, 468 amino acids
Four ‘levels’ of protein structure
Four levels of protein structure
Primary structure: Visualized as a straight chain of aa’s, but with a specific sequence, As determined by its gene
Secondary structure: alpha helix or beta pleated sheet
Tertiary structure: coiled chains of aa’s are folded & wound around themselves
Close up of 2 o & 3 o Protein Structure
Quarternary structure: separate polypeptide chains are combined
Levels of Protein Structure
Four Levels of Protein Structure (note change in scale from 2 o to 3 o )
Collagen molecule
Actin molecule
Myosin molecule
Hemoglobin molecule
Antibody molecule
(purple) Reverse transcriptase of HIV1 w/ a fragment of DNA (colors)
Protein Synthesis: Transcription & Translation
Transcription: Making a copy of the blueprint
Morse Code Key
Using the Genetic Code: DNA :: mRNA :: Protein Get from ‘language’ of DNA (A,G,C,orT) to ‘language’ of protein (aa’s) DNA’s ‘language’ is a triplet code in which 3 nucleotide bases (a codon) specify 1 amino acid in protein.
DNA (1 gene) :: mRNA :: polypeptide
Steps in Transcription
Transcription: Note the free nucleotides
DNA unzips
Complementary base pairing
mRNA- final product of Transcription mRNA moves off to ribosome
Transcription: Getting the plan straight (copying the gene)
Transcription animation
Translation Building the protein from the plan
Using the Genetic Code: DNA :: mRNA :: Protein Get from ‘language’ of DNA (A,G,C,orT) to ‘language’ of protein (aa’s) DNA’s ‘language’ is a triplet code in which 3 nucleotide bases (a codon) specify 1 amino acid in protein.
Structure of a Ribosome
Structure of a tRNA
Translation : purple = mRNA blue = ribosome yellow = tRNA (note anticodon) white = amino acids red = peptide bond
Translation initiation
Translation initiation (cont)
Translation- elongation
Translation- termination
A Polysome: With more than one ribosome translating an mRNA at one time, it is possible to produce many polypeptides simultaneously from a single mRNA.
Protein Synthesis
In a prokaryotic cell, transcription and translation are coupled; that is, translation begins while the mRNA is still being synthesized. In a eukaryotic cell, transcription occurs in the nucleus, and translation occurs in the cytoplasm.
Protein synthesis in eukaryotes
Antibiotic Mechanism
Antibiotic Mechanism
Collagen molecule
Actin molecule
Myosin molecule
Antibody molecule
Hemoglobin molecule
Enzymes
Definitions: Catalyst = An additive that speeds up a chemical reaction without itself being consumed or changed by the reaction Enzyme = A protein that acts as a catalyst, usually in a biological context. –All enzymes are proteins, not all proteins are enzymes
Enzyme mechanism of action: An enzyme improves the odds of ‘useful’ collisions between substrate molecules.
Steps in enzyme function
Enzyme-substrate animation
S = substrate E = enzyme P = product ES = enzyme- substrate complex
Lock & Key Model: Enzymes are very specific and it was suggested by Emil Fischer in 1890 that this was because the enzyme had a particular shape into which the substrate(s) fit exactly. This is often referred to as "the lock and key" hypothesis. An enzyme combines with its substrate(s) to form a short- lived enzyme-substrate complex.
Induced fit hypothesis: In 1958 Daniel Koshland suggested a modification to the "lock and key" hypothesis. Enzymes are rather flexible structures. The active site of an enzyme could be modified as the substrate interacts with the enzyme. The amino acids side chains which make up the active site are molded into a precise shape which enables the enzyme to perform its catalytic function. In some cases the substrate molecule changes shape slightly as it enters the active site. A suitable analogy would be that of a hand changing the shape of a glove as the glove is put on.
Enzyme Animation
Enzyme Websites: Enzyme notes in ppt format, few diagrams: animation of enzyme action written outline- enzymes by Worthington asd
Enzyme & Cell Regulation Gene activation Feedback loops for enzyme activity
Various possible routes of feedback in the production-regulation of a given protein
Changing the conformation (shape) of an enzyme’s active site changes its ability to act as a catalyst
Zymogens: Enzyme Precursors
Competitive Enzyme Inhibition
Allosteric Modulation of an Enzyme
Genes can be either inducible or repressible. Many genes are normally blocked by the action of a repressor protein. This prevents the RNA polymerase enzyme from binding to the gene and transcribing the structural gene. Such genes are induced by the arrival of an inducer molecule which binds to the repressor protein and rendering it inactive. This allows transcription from the structural gene and the production of a protein. Other genes are normally active and able to be constantly transcribed, because the repressor protein is produced in an inactive form. On the arrival and binding of the corepressor molecule the complex can act as a functional repressor and block the structural gene by binding at the operator site.
Steps in Transcription
DNA Technology
Bases: A- adenine G- guanine T- thymine C- cytosine
Other translation animations: Add an amino acid to tRNA- Initiation of Translation- Elongation of Polypeptide- Termination of Polypeptide-