pre-release Flashcards
What type of bond is a Hydrogen bond?
An intermolecular bond
What’s an intermolecular bond?
A bond forming between molecules (not within them)
What are the three atoms that a H must be attached to for Hydrogen bonding to occur?
Oxygen
Fluorine
Nitrogen
Explain why ethanol has hydrogen bonds
- O more electronegative than H on hydroxyl group
- Meaning O has the electrons pulled closer towards it and away from the H- forming a dipole (delta+ H and delta- O)
- This causes attraction between the delta positive and delta negative Hs and Os on other ethanol molecules, forming Hydrogen bonds
Why won’t a H bonded to a C hydrogen bond?
There’s not a large enough difference in electronegativity, therefore no dipole.
How does Hydrogen Bonding affect Boiling Point?
More hydrogen bonding= higher boiling point
What’s electronegativity?
A measure of an atoms ability to attract the shared pair of electrons in a covalent bond
How does electronegativity vary in the periodic table?
It increases going across a period
It decreases going down a group
Why is it that substances with stronger IM bonds have higher boiling points?
It requires more energy to overcome these bonds
What are permanent dipoles?
When there’s a difference in electronegativity in a molecule so one atom will always be delta+ and the other delta-
What’s an instantaneous dipole?
The electron loud is always moving throughout a molecule so at some point it will happen to be more at one end of the molecule and form an instantaneous dipole with one part delta- and the other delta+
What’s an induced dipole?
When a non-polar molecule e.g. Cl2 is next to either a permanent dipole or an instantaneous dipole, which induces a dipole in the non-polar molecule
Give the 4 types of IM bond:
- Permanent dipole-permanent dipole
- Instantaneous dipole-induced dipole
- Permanent dipole- induced dipole
- Hydrogen bond
What’s a Hydroxyl group?
an O-H group
What’s an enantiomer the same as?
An optical isomer
What’s the general structure of an Amino Acid?
Central C, with an amine (NH2) group attached, as well as an H, a carboxyl group and a varying R group (depending on the Amino Acid)
What’s an alpha-amino acid?
When the amine and the carboxyl groups are bonded to the same carbon
What’s a beta-amino acid?
When there’s two central carbons, so the carboxyl and amine groups are bonded to different carbons
What’s a zwitterion?
Where an amino acid reacts with itself with the H+ from the carboxyl group leaves (forming COO-) and goes to the Amine group (forming NH3+)
What are the two important points about zwitterions?
- They have no overall charge
- They form at a specific isoelectric point (pH) which is different for each amino acid.
In acidic conditions, what does an amino do when in acidic conditions?
The Carboxylic acid group keeps its H and the NH2 group gains a H+- forming NH3
In basic conditions what happens to a amino acid?
The carboxylic acid group loses a H (leaving COO-) and any carboxyl groups in the R group will lose their H
What’s the reaction joining Amino Acids called?
condensation reaction
What’s the bond between Amino acids called?
peptide bond
What’s a polypeptide?
Many amino acids in a chain joined by peptide bonds
What’s a protein?
50+ amino acids joined by peptide bonds
What’s the primary structure of a protein?
The arrangement/chain of amino acids in a polypeptide.
What are the products of acid hydrolysis of an ester?
Alcohol + Carboxylic Acid