Organic Synthesis,NMR And Amino acids Flashcards
What do amino acid molecules consist of and what property do they share
An amine group
A carboxylic acid group
They are all chiral
State the properties that the carboxylic acid and amine group have in Amino acid and state what they react with
Carboxylic acid has acidic properties and so react with bases
Amines have basic properties and react with acids
What would happen when the amino acid is in a high ph(alkali)
The COOH would lose a hydrogen and become
COO-
What would happen when the amino acid is in a low ph (reacts with acids)
The Nh2 would gain a hydrogen
Becomes NH3+
What is is called when amino acid reacts with itself
It’s referred to an a zwitterion they have both a proton donar(COOH)and proton accepting group(NH3)
NH3 +
COO-
State the bond that forms between amino acids in a protein
Peptide bonds
What is the primary structure of a proteins
The sequence of amino acids in a chain
What are the two secondary structures proteins can form
A helix
Beta plated sheets
State why secondary structures can occur in proteins
As hydrogen bonds can occur between the hydrogen atom on peptide link with either a nitrogen or oxygen on another peptide link
What is the tertiary structure and how does it occur
The 3D structure of a protein it occurs as a result of interactions between amino acid groups further apart in the chain
State the 3 types of bonds that can form in the tertiary structure
Hydrogen bondings
Ionic bonding
Covalent sulfur Sulfur bonds (disulphides Bridge
What are the 4 bases in DNA
Adenine
Cytosine
Guanine
Thymine
What is DNA made up of
Phosphate ion
2-deoxyribose
One of the four bases(adenine,cystine,guanine,thymine)
State the complementary bonding in DNA
Thymine pairs with adenine
Cytosine pairs with Guanine
When a condensation reaction occurs between two nucleotides what is formed and where does the bond occur
It occurs between the phosphate group of one nucleotide and the deoxyribose of another it’s a covalent bond
What is the function of cisplatin and give its structure
It’s anti-cancer drug
- 2(Cl)-Pt-(NH3)2
How does cisplatin work
It binds to two of the Guanine bases on a strand of DNA
It undergos ligand substitution with with the Nitrogen on Guanine replacing the CL on the cisplatin and a dative covalent bond forms
This action prevents cell replication of the DNA which means cancer cells can no longer divide
Why does the Nitrogen atom on the cisplatin replace the Chlorine on the cisplatin
As it’s a better ligand
State why cancer drugs like cisplatin have side effects
Because it binds to DNA in healthy cells preventing them from replicating and so as a result people may lose their hair
What are enzymes
That are globular proteins that catalyse reactions
What part of an enzyme catalyses reaction
It’s active side
Why are enzymes considered to be stereospefic
As their 3D shapes can only catalyse one individual enantiomer or pair of a chiral molecule
What happens in enzyme inhibition.
drugs are designed that have a similar shape to the substrate,
It will bind to the active site of the enzyme blocking the substrate from binding it preventing a reaction occurring so the reaction won’t occur
Why are computer models becoming useful in treating enzymes
They can predict the shape of the enzyme and once the shape is understood then they can design the shape of the substrate that can react with the enzyme
Why is enzyme inhibition useful
As we can prevent the reaction of enzymes that may cause harmful reactions in our body
State how the structures in a protein can be identified and give the name of the process and the reagent involved
By hydrolysis using 6 mol dm of hydrochloric acid
This breaks the amide bond in the protein
Why is TMS used as standard and state it’s formula
It’s inert
Non-toxic
Low melting point so it
can be removed easily
Produces a single peak as all the hydrogens are chemically equivalent
Produces an intense peak
Si(ch3)4
What is the standard used in proton nmr and why it is useful
CCl4,CDCL3 is the isotope
Contains no hydrogens atoms
What is the advantages of Tlc over papar chromatography
It runs faster
Smaller amounts of mixture can be separated
Spots spread out less
What is the mobile phase in chromatography
It’s carries the soluble components of the mixture with it
Give the 3 types of chromatography
Thin layer chromatography
Column chromatography
Gas chromatography
What happens in column chromatography
A glass tube (which is the column) is filled with the stationary phase (slica)in powder form to increase the surface area
A filter is used to retain the solid in the tube
The mixture to be analysed is to be dissolved in the solvent and is then add EE to the column
The solvent is then run through the column
The time for each component in the mixture to reach the column is recorded
What is retention time and why is it useful
The time for each component to reach the end of the mixture
It can be used to identify a component
What happens in gas chromatography
A gaseous mixture is injected into a column and is allowed to flow through under high pressure
The time it takes to control exit the coloumn is called retention time and can be used to identify the component
In gas chromatography what is the mobile phase and stationary phase
Gas like helium
A liquid with a high boiling point
State how haloalkane are formed
From electrophillic addition of alkenes
State what the splitting patterns
Singlet
Doublet
Triplet
Quartet dhow
Singlet-shows that the adjacent carbon has no hydrogen attached(indicating possible functional group)
Doublet shows the adjacent carbon has 1 hydrogens
Triplet shows that the adjacent carbon has 2 hydrogens
Quartet shows that the adjacent carbon has 3 hydrogens attached
What do the amount of peaks on carbon nmr tell us
The number of different environments carbon is in
