Analytical Chemistry II

GENERAL OBJECTIVES:

1. Understand the principle, operation and application of NMR Spectroscopy

2. Understand the principles, operations and applications of mass spectroscopy

3. Understand the principles, operations and applications of X-ray diffraction

4. Understand the principles, operations and applications of surface analysis techniques

5. Understand the basic principles and applications of Biosensors

1.1 Explain the fundamental principles of the NMR technique.

1.2 Draw a schematic diagram of the NMR Spectrometer.

1.3 Describe the basic principles of NMR spectrometer.

1.4 List the important nuclei used for NMR (spin-1/2 nuclei)

1.5 Explain the term: chemical shift.

1.6 Understand how to calculate intensity using the integral of the signal curve.

1.7 Explain the terms: spin-spin coupling, spin-decoupling.

1.8 Discuss the use of fourier transform in NMR

1.9 Describe the chemical shifts from common organic compounds for 1H nuclei

1.10 Describe the chemical shifts from common organic compounds for 13C nuclei

1.11 Discuss the type of information that can be gained from spin-spin coupling constants (J numbers)

1.12 Explain the applications of NMR spectroscopy.

2.1 Draw a schematic diagram of a Mass Spectrometer.

2.2 Describe the working principle of a mass spectrometer.

2.3 Understand the differences between the three concepts of mass used in MS: average, nominal and exact molecular mass.

2.4 Discuss the types of ion sources used in MS: electron impact ionisation, chemical ionisation, atmospheric-pressure chemical ionisation, fast atom bombardment, thermospray, electrospray.

2.5 Discuss the types of analysers used in MS: single-focusing magnetic instruments, doublefocusing instruments, quadrupole analysers, Time of Flight (ToF) analysers, ion-trap analysers

2.6 Discuss the use of an electron multiplier as a detector for MS and the conversion to detect negative ions

2.7 Describe the procedure for recording the mass spectrum of a sample.

2.8 Discuss the three type of data output that may be obtained using a MS: total-ion chromatogram, mass chromatogram, mass spectrum.

2.9 Describe other applications of mass spectroscopy.

2.10 Describe the use of mass spectra in qualitative analysis of a mixture.

2.11 Discuss the use of coupled MS techniques such as ICP-MS, GC-MS and LC-MS

3.1 Describe the X-ray diffraction method.

3.2 Discuss the two classes of symmetry operations used to describe the internal arrangement of atoms or molecules in crystals: proper and improper

3.3 Discuss the seven crystal systems and their unit cells

3.4 Discuss the use of Bragg reflections and structure factors for structural analysis

3.5 Discuss the analytical applications of powder diffraction

4.1 Discuss the characteristic surface features that can help determine the properties of a material: topology and morphology, elemental composition, chemical bonding of elements, structure (geometric and electronic)

4.2 Discuss the three main types of photon probe techniques: scattering, absorption and emission. Give examples for each at the different spectral ranges

4.3 Understand the principles of photoelectron spectroscopy including UPS and XPS

4.4 Draw a schematic of an XPS instrument

4.5 Discuss the major differences between UPS and XPS

4.6 Discuss the principles and applications of Laser Micro Mass Spectrometry (LAMMS)

4.7 Identify the main differences between photon probe and electron probe techniques

4.8 Discuss the fundamental principles of electron penetration of material and elastic and inelastic interaction with matter

4.9 Draw a simple diagram of the configuration of an scanning electron microprobe for secondary and back-scattered electron imaging and X-ray analysis

4.10 Discuss the use of secondary and back-scattered electron imaging and the differences between these two methods

4.11 Discuss the principles and applications of transmission electron microscopy

4.12 Discuss the basic principles of ion probe techniques

4.13 Discuss the different ion probe techniques used for elastic and inelastic processes

4.14 Discuss the applications of scattering and sputtering ion probe techniques

4.15 Understand the three fundamental processes involved in field probe techniques: field ionisation, electron tunnelling, interatomic force interaction.

4.16 Understand the principles of scanning tunnelling microscopy (STM)

4.17 Discuss the type of information that can be gained from a STM image: topography, electronic structure

4.18 Discuss the different operational modes of STM identifying the differences in the information gained

4.19 Discuss the principles of Atomic Force Microscopy

4.20 Discuss the different operational modes of AFM (constant force and constant height)

4.21 Discuss the different information that can be obtained using the AFM: topography, deflection, phase lag, interactive forces, magnetic properties, conducting properties

4.22 Discuss the principles of forcedistance curves using AFM

4.23 Discuss the principles of tapping mode for analysis of delicate samples

4.24 Understand the principles of phase lag imaging using tapping mode AFM

4.25 Discuss the applications of AFM

5.1 Understand what separates a biosensor from any other chemical sensor

5.2 Discuss the use of a biorecognition agent to give selectivity for the analyte

5.3 Discuss the immobilisation of the biorecognition agent: physical adsorption, physical retention in polymer matrices, surface modification. Highlight issues with applying the immbolisation layer to the sensor surface

5.4 Discuss the principles of enzyme electrodes

5.5 Using the glucose oxidase enzyme as an example discuss the reaction pathways for amperometric measurement via a redox mediator

5.6 Discuss the use of NAD-linked enzyme electrodes

5.7 Discuss the basic principles of optical biosensors; intrinsic and extrinsic

5.8 Understand the principles of labelled assays for optical detection

5.9 Discuss techniques that can be used to amplify optical changes in unlabelled assays: interference techniques, grating couplers, surface plasmon resonance (SPR)