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Spectroscopy of biomolecules
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Spectroscopy of biomolecules
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Academic year 2023/2024
- Course ID
- BIO0153B Pds 308-BIDD
- Teachers
- Simonetta Geninatti Crich
Gloria Berlier - Degree course
- [0101M22] Molecular Biotechnology
- Year
- 1st year
- Teaching period
- First semester
- Type
- Distinctive
- Credits/Recognition
- 5
- Course disciplinary sector (SSD)
- CHIM/02 - physical chemistry
CHIM/03 - general and inorganic chemistry - Delivery
- Formal authority
- Language
- English
- Attendance
- Obligatory
- Type of examination
- Written and oral
- Type of learning unit
- modulo
- Modular course
- SUPRAMOLECULAR CHEMISTRY AND SPECTROSCOPIC METHODS (BIO0153 Pds 308-BIDD)
- Prerequisites
- The students should have acquired the basic knowledge in Inorganic Chemistry, Physical Chemistry, Biochemistry
- Propedeutic for
- All courses and practical activities dealing also with methods based on molecular spectroscopies
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Sommario del corso
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Course objectives
Spectroscopic methods play an increasingly important role in studying the molecular details of complex biological systems in health and disease. However, no single spectroscopic method can provide all the desired information on aspects of molecular structure and function in a biological system but the simultanous use of different methods.
The objectives proposed to students in this course are based on the following achievements:
1. knowledge of the chemical, physical and physical-chemical principles at the basis of the generation of signals exploited in molecular spectroscopies of biomolecules (small molecules and macromolecules), namely NMR spectroscopy, electronic spectroscopies (both in absorption and emission) and vibrational spectroscopy (main concepts)
2. good capability in critical understanding scientific texts
3. good capability in designing investigation of different samples by molecular spectroscopies, on the basis on their constitutive features, possible constrains related to limited amounts, types of outputs requested (identification; quantification)
4. good capability in the complementary use of the molecular spectroscopic methods indicated above
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Results of learning outcomes
At the end of the coruse the students will be able to:
- Handle the main methods for NMR and electronic spectroscopic (both in absorption and emission) measurements
- Design proper spectroscopic measurements for the investigation of biomolecular samples, taking into account the peculiar features of these samples (e.g, complexity of the matrix), and the specific target(s) to be pursued (identification/quantification)
- Manage the fundamentals of electronic spectroscopies.
- Analyse data resulting from the methods indicated above.
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Program
Infrared spectroscopy for the study of proteins
Absorption electronic spectroscopy:
- origin of the energy transfer from the electromagnetic radiation to molecular electronic states
- types of electronic levels and electronic transitions
- solvatochromism
- UV circular dichroism
- study of the protein structure by absorption electronic spectroscopy (principles, experimental methods)
- study of the structure of nucleic acids by absorption electronic spectroscopy (principles, experimental methods)
Photoluminescence electronic spectroscopy:
- radiative and radiation less decays from excited electronic states
- fluorescence and phosphorescence
- radiative and fluorescence lifetimes
- collisional quenching
- energy transfer through the space
Nuclear Magnetic Resonance (NMR) Spectroscopy applications in the determination of structure, dynamics, and interactions of biological molecules and macromolecules:
- Introduction to the NMR spectral parameters used in structural biology, namely the chemical shift, the J-coupling, nuclear Overhauser effects, and residual dipolar couplings.
- Resonance assignment, and NMR spectral parameters are their convertion into angle and distances between atoms in a macromolecules.
-Relaxation phenomena and mapping the molecular interactions, information on the binding interface as well as the determination of kinetic and thermodynamic constants..
- In cell/In tissue NMR spectroscopy.
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Course delivery
The course will be delivered through lessons in the lecture room (90%) and in labs (10%), for focus on some methodological aspects.
Part of the course will be devoted to NMR (3 CFU, 24 h) and part to electronic (absorption and emission) spectroscopy (2 CFU, 16 h)- Oggetto:
Learning assessment methods
The exam is devoted to the assessment of the knowledge, and related understanding, of the program attained by the students. In addition, acquisition and understanding of basic knowledge in Chemistry and Biochemistry will be evaluated if necessary in relation to the program, as well as the use of a proper scientific/technical language.
The exam on electronic spectroscopies will be in oral form with Prof. Berlier.
The exam on Nuclear Magnetic Resonance will consist in a written examination with Prof. Geninatti Crich. The final mark is expressed in thirtieths.
Suggested readings and bibliography
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Reference material is available at the course website.
Suggested textbooks (all available from the teachers):
- H. Friebolin “Basic one- and two-dimensional NMR spectroscopy”, VCH, 1993
- Ivano Bertini, Kathleen S. McGreevy, Giacomo Parigi “NMR of biomolecules” Wiley 2012.
- DW. Claridge “High-resolution NMR techniques in Organic Chemistry”, Pergamon 1999 (Elsevier Science)
N.J. Turro, Modern Molecular Photochemistry, University Science Books, 1991
C.N.R. Rao, Ultra-Violet and Visible Spectroscopy, Butterworths, third edition, 1966
J.R. Lakowitz, Principles of fluorescence spectroscopy, Plenum, 2000 I.D. Campbell
- Enroll
- Open
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