Course Overview

The objective of this lecture is to provide to each student both
theoretical and practical tools enabling him to correlate the
experimental data obtained from different analytical techniques and
structures mainly in solution of molecular and macromolecular
architectures. 
Special attention will be paid to the acquisition, the rationalization
and the interpretation of high-resolution NMR, mass, Raman and IR
spectra with examples taken from major application domains such as
structure determination of organic compounds, lipidomics, and
proteomics. 

Furthermore, both the use and applications of static and dynamic light
scattering will be highlighted to characterize macromolecules in
solution along with nanoparticle suspensions. 

Learning Achievement

Competence

Course prerequisites

- Academic level: BSc
- Selection criteria: basic knowledge in chemistry, physical
chemistry and analytical chemistry
- Language prerequisites: English or French
- Selection procedure: evaluation of the students CV

Grading Philosophy

> The first session will take place in December

- Intermediate written exam: 2h = 33 % of the overall mark
- Written final exam: 3h = 67 % of the overall mark 

>In case of failure, a second session will be organized for the final
exam: Written or oral exam (depending on the student body if written
exam 3h) = 67 % of the overall mark

- Continuous control: report left to the student's choice depending
on its first marks. In case of choice to retake the exam: written test
(2h) or oral following effective = 33 % of the overall mark

Course schedule

PART 1: HIGH RESOLUTION NMR
I. Principles of nuclear magnetic resonance:

- Quantum model (nuclear spin, nuclear magnetic moment, energy of a
nuclear spin in a magnetic field, sensitivity, receptivity, etc.).
- Vector model (the rotating frame).
- Fourier Transform Pulse Spectroscopy (pulse production, pulse mode,
FID, FT, spectrum, relaxation processes).

II. Spectral parameters and analyses of spectra:

- Chemical shift (origin, rationalization, application in 1H and 13C
NMR°.
- Quantitative analysis (integration).
- Coupling processes (types, origin, examples, application to the
molecular structure determination).

III. 1D NMR: Multi-impulsional NMR sequences:

- Double resonance techniques (homonuclear and heteronuclear
decoupling, NOE effect, examples).
- Multi-impulsional 1D NMR sequences (Spin-Echo, J-modulated
Spin-Echo, DEPT).

IV. 2D NMR: Basic concepts and applications:

- Introduction to 2D NMR (Principle, Time-scale in 2D NMR
experiments, 2D FT, Various Plots).
- Examples of 2D NMR experiments (J-Resolved, COSY, HMQC, HSQC, HMBC,
NOESY, ROESY).

PART 2: MASS SPECTROMETRY

- Ionisation modes: electron impact ionisation, chemical ionisation,
photoionisation, matrix assisted laser desorption-ionisation,
electrospray.
- Principles of mass analyzers (quadripole, ion trap, time of flight,
orbitrap, Fourier transform Ion cyclotron resonance)
- Principles of tandem mass spectrometry (MS/MS) including various
modes of fragmentations (Collision Induced Dissociation, Electron
Transfer/Capture Dissociation, InfraRed Multiple Photon
Dissociation...)
- Coupling with chromatography (gas and liquid).
- Principles of quantitative analysis by mass spectrometry (selected
Ion Monitoring, Multiple Reaction Monitoring).
- Applications: complex matrices (environmental, biological),
lipidomics, proteomics, imaging.

PART 3: VIBRATIONAL SPECTROSCOPY AND IMAGING MATERIALS

I. Basic principles of optical spectroscopies

   1.1-Fundamental aspects of light/matter interaction.

   1.2-Optical spectroscopies.

II. Molecular Symmetry
   2.1-Molecular symmestry and point groups

   2.2-Using symmetry to predict vibrational activity

III. Spectroscopic Analysis of Vibrational Spectra:

   3.1-General Principles

   3.2-Examples

IV. Raman Scattering

   4.1- Spontaneous Raman scattering

   4.1-Polarized Raman spectroscopy

   4.3-Micro-Raman and Imaging

V. Fourier Transform InfraRed (FTIR) absorption spectroscopy

   3.1-FTIR spectroscupy

   3.2- Transmission and reflection techniques

   3.3- IR microscopy and imaging

PART 4: LIGHT SCATTERING

I. Introduction to light scattering:

- Origin of the light scattering process.
- Reciprocal space and scattering vector.

II. Static light scattering:

- Very small particles (d

Course type

- Lectures (main lectures are taught in French but all written supports are available in English or French):  26 x 1 hour and 20 minutes. - Exercise sessions (in French or English): 12 x 1 hour and 20 minutes. - Tutoring (in English to help students who do not speak French): 9 x 1 hour  and 20 minutes. - Self-study: 85 hours (30 hours private reading, 20 hours exam preparation, 35 hours exercise preparation. - Teaching supports available on the Moodle platform.

Online Course Requirement

Instructor

Other information

* Main lectures will be taught in French but all written supports will
be available in English or French (lectures, exercises, practical
sessions manuals, final exam written texts )
Tutoring in English will be available to help people who do not speak
Frenchiii

Exercise sessions will be taught in both English or French 



Language of instruction: French and English* (see other information)
Mode of delivery: Face-to-face teaching

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