Overview: Organic Chemistry Flashcards

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1
Q

Chemical Bonds Strong Bonds Intramolecular

A

Ionic Covalent (Metallic) Greater than >100kJ/mol

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2
Q

Chemical Bonds Intramolecular Weak Bonds

A

Hydrogen (10-50 kJ/mol) Van der Waals <10kJ

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3
Q

Electron shells Unfilled

A

Unfilled electron shells are unstable.

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4
Q

Electron shells How do atoms get filled electron shells?

A

Accepting / Donating Sharing

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5
Q

Ionic bonding

A

Accepting / Donating

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6
Q

Convalent Bonding

A

Sharing

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7
Q

What is Electronegativity

A

Measure of an atom’s ability to attract electrons in a molecule.

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8
Q

What is electronegativity dependent on?

A

Strength of positive charge in nucleus Distance of bonded electrons (shielding from electron shells)

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9
Q

Polar molecules Dipoles

A

Molecules with higher electronegativity draw the electrons closer to themselves and away from their neighbours.

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10
Q

Van der Waals forces

A

Attractive or repulsive forces formed by dipoles Much weaker than covalent bonds Only work at short distances.

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11
Q

Hydrogen Bonds Possible with dipole?

A

Possible with dipole where hydrogen bonds to a highly electrnegative atom.

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12
Q

What is a dipole?

A

a pair of equal and oppositely charged or magnetized poles separated by a distance.

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13
Q

Hydrogen Bonds Features

A

Relatively positive. Attracts negative atoms. Weaker than covalent bonds. Stronger than Van der Waals Vital for DNA and protein structure

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14
Q

Ionic Bonds Summary

A

Donation of electrons from one (metal) atom to another (non-metal) to form positive and negative ions which then attract.

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15
Q

Covalent Bonds Summary

A

Sharing of electron pairs (non-metals)

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16
Q

Van der Waals bonds Summary

A

Weak attractions of covalent dipoles

17
Q

Hydrogen Bonds Summary

A

Attractions of covalent dipoles involving hydrogen covalently bonded to a highly electronegative atom

18
Q

Chemical bonds Summary

Strength equation

A
19
Q

What is molecular geometry?

A

3D arrangement of atoms in a molecule.

Affects reactivity, polarity, state of matter, colour, etc.

Electrons (bonded or free pairs) repel; they try to stay as far away from each other as possible.

20
Q
A
21
Q

Molecular Geometry

3 Bonds

A

Planar

22
Q

Molecular Geometry

Four bonds

A

Tetrahedral

23
Q

Molecular Geometry

2 Bonds

A

Linear

24
Q

Molecular Geometry

When does bond rotation occur?

A

Only occurs around single bonds.

Less energetically favourable

25
Q

Carbon-based Life

Advantages of Carbon

A

Abundant

Versatile - 4 Valent

Small

Good bond strength

Physical structure - chains

26
Q

Next best thing to use after Carbon?

A

Silicon

27
Q

Structure of H2O

A

“Bent”

Polar molecule

Hydrogen bonds lead to a lattice structure

28
Q

What is the Hydrophoic effect?

A

Not fully understood

Engergetically unfavourable disruption of hydrogen bonding

Hydrophobic elements aggregate to minimise disruption

Effect tends to be stronger than Van der Waals or hydrogen bonds

Hydrophoic effect is vital to protein structure

29
Q

Dissociation of Water

H2O

A

H2O = H+ OH-

Hydrogen ions can then bind to undissociated H2O to form hydronium ions (H3O+)

H20 + H20 = H3O+ + OH-

Water donates and accepts H+, so it is both an acid and a base.

30
Q

pH “power of hydrogen”

A

pH = -log10[H+] = log 1 / [H+]

If [H+] = 1 x 10-^7, PH = 7

A change in pH of 1 represents a tenfold change in [H+]

31
Q

Acids, bases, buffers

What is pH regulation vital for?

A

Biochemical processes

32
Q

Acids, bases, buffers

Acids

Hydrogen

A

Acids donate hydrogren ions; increase [H+]

33
Q

Acids, bases, buffers

Bases

Hydrogen

A

Accept hydrogen ions

Decrease [H+]

34
Q

Acids, bases, buffers

What do buffers do?

A

Provide small pH changes in response to moderate amounts of acid / base.

Mixture of weak acid (HA) and conjugate base (A-) or weak base (B) and conjugate acid (HB+)

35
Q

Henderson-Hasselbalch Equation

pKa

A

The lower pKa is, the stronger the acid.

Weak acids have pKa in the range of -2-12

36
Q

Physiological Buffers

A

Bicarbonate: H2CO3 pKa - 6.1

Phosphate: H2PO24^2- pKa - 7.2

Proteins

(Haemoglobin pKa - 6.6 - 8.2)

37
Q
A
38
Q

Physiological Buffers

Normal Human pH

A

Human 7.3

Plasma <6.8 - >7.8 may be fatal.