Consiglia TEDESCO | CRYSTALLOGRAPHY

cod. 0522300049

CRYSTALLOGRAPHY

	0522300049
	DEPARTMENT OF CHEMISTRY AND BIOLOGY "ADOLFO ZAMBELLI"
	EQF7
	CHEMISTRY
	2023/2024

CURRICULUM BIOMOLECULAR CHEMISTRY

	YEAR OF COURSE 2
	YEAR OF DIDACTIC SYSTEM 2016
	SPRING SEMESTER

TEACHING UNITS

SSD	CFU	HOURS	ACTIVITY	TYPE OF ACTIVITY
CHIM/02	4	32	LESSONS	SUPPLEMENTARY COMPULSORY SUBJECTS
CHIM/02	2	24	LAB	SUPPLEMENTARY COMPULSORY SUBJECTS

	Objectives
	THE AIM OF THE COURSE IS INTRODUCING THE STUDENT TO THE FUNDAMENTAL PRINCIPLES OF THE STRUCTURAL CHARACTERIZATION OF BIOMOLECULES, IN PARTICULAR X-RAY DIFFRACTION AND ELECTRON MICROSCOPY TECHNIQUES. THE ACQUIRED KNOWLEDGE WILL ALLOW THE STUDENT TO ANALYZE AND DISCUSS AT THE ATOMIC LEVEL THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS AND OTHER MOLECULES OF BIOLOGICAL INTEREST. THE STUDENT WILL BE ABLE TO UNDERSTAND THE STRATEGIES AND LIMITATIONS OF THE DIFFERENT METHODS.

THE AIM OF THE COURSE IS INTRODUCING THE STUDENT TO THE FUNDAMENTAL PRINCIPLES OF THE STRUCTURAL CHARACTERIZATION OF BIOMOLECULES, IN PARTICULAR X-RAY DIFFRACTION AND ELECTRON MICROSCOPY TECHNIQUES.
THE ACQUIRED KNOWLEDGE WILL ALLOW THE STUDENT TO ANALYZE AND DISCUSS AT THE ATOMIC LEVEL THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS AND OTHER MOLECULES OF BIOLOGICAL INTEREST. THE STUDENT WILL BE ABLE TO UNDERSTAND THE STRATEGIES AND LIMITATIONS OF THE DIFFERENT METHODS.

	Prerequisites
	A BASIC KNOWLEDGE OF GENERAL CHEMISTRY, ORGANIC CHEMISTRY AND BIOCHEMISTRY.

	Contents
	THE COURSE CONSISTS OF 56 HOURS (32 HOURS LECTURE + 24 H LABORATORY) THE TOPICS ADDRESSED IN 56 HOURS (32 LECTURE + 24 LABORATORY) ARE: INTRODUCTION TO CRYSTALLOGRAPHY. CRYSTALLINE SOLIDS. UNIT CELL AND ASYMMETRIC UNIT. SYMMETRY ELEMENTS. (8 H LECTURE + 6 H LABORATORY) CRYSTALLIZATION OF NUCLEIC ACIDS AND PROTEINS. EXPERIMENTAL TECNIQUES FOR THE CRYSTALLIZATION OF BIOLOGICAL MACROMOLECULES.VAPOUR DIFFUSION CRYSTALLIZATION (HANGING DROP, SITTING DROP), DIFFUSION CRYSTALLIZATION, BATCH CRYSTALLIZATION.“HIGH THROUGH-PUT” CRYSTALLIZATION. CRIOCRYSTALLOGRAPHY. CRYOPROTECTORS. (6 H LECTURE + 6 H LABORATORY) DATA COLLECTION. RADIATION AND MATTER. X-RAY DIFFRACTION. X-RAY SOURCES: X-RAY TUBES AND SYNCHRTRON LIGHT. X-RAY DETECTORS: CCD AND IMAGE PLATE.ROTATING CRYSTAL METHOD. (6 H LECTURE + 3 H LABORATORY) HOW TO SOLVE THE STRUCTURE: THE PHASE PROBLEM. STRUCTURE FACTOR AND ELECTRON DENSITY. HEAVY ATOM METHOD, SIR, MIR, MOLECULAR REPLACEMENT, SAD, MAD. ELECTRON DENSITY MAPS. CRYSTALLOGRAPHIC DISAGREEMENT INDICES. (4 H LECTURE + 3 H LABORATORY) CRYSTALLOGRAPHIC DATABASES. PROTEIN DATA BANK. CARTESIAN COORDINATES AND CRYSTALLOGRAPHIC COORDINATES. PDB FILES. PROGRAMS FOR THE VISUALIZATION OF CRYSTAL STRUCTURES. (4 H LECTURE + 3 H LABORATORY) ELECTRON MICROSCOPY AND ELECTRON DIFFRACTION. (4 H LECTURE + 3 H LABORATORY) THE TOPICS ADDRESSED IN MODULE B ARE: GENERAL PRINCIPLES OF SPECTROSCOPY. NUCLEAR MAGNETIC RESONANCE., 1H-NMR AND 13C-NMR AND MULTIPULSE MULTIDIMENSIONAL NMR TECHNIQUES (12H LECTURE, 10H LABORATORY). MASS SPECTROMETRY: INTRODUCTION, IONISATION PROCESSES, FRAGMENTATION PROCESSES (8H LECTURE, 6H LABORATORY), APPLICATIONS. ULTRAVIOLET AND VISIBLE SPECTROSCOPY: MOLECULAR ORBITAL AND ELECTRONIC TRANSITIONS, CHROMOPHORES,APPLICATIONS (6H LECTURE, 4H LABORATORY). INFRARED SPECTROSCOPY, MOLECULAR VIBRATIONS ,STRUCTURAL INFORMATIONS IN MACROMOLECULES WITH VIBRATIONAL SPECTROSCOPY (6H LECTURE, 3H LABORATORY).

Contents

THE COURSE CONSISTS OF 56 HOURS (32 HOURS LECTURE + 24 H LABORATORY)

THE TOPICS ADDRESSED IN 56 HOURS (32 LECTURE + 24 LABORATORY) ARE:
INTRODUCTION TO CRYSTALLOGRAPHY. CRYSTALLINE SOLIDS. UNIT CELL AND ASYMMETRIC UNIT. SYMMETRY ELEMENTS. (8 H LECTURE + 6 H LABORATORY)
CRYSTALLIZATION OF NUCLEIC ACIDS AND PROTEINS.
EXPERIMENTAL TECNIQUES FOR THE CRYSTALLIZATION OF BIOLOGICAL MACROMOLECULES.VAPOUR DIFFUSION CRYSTALLIZATION (HANGING DROP, SITTING DROP), DIFFUSION CRYSTALLIZATION, BATCH CRYSTALLIZATION.“HIGH THROUGH-PUT” CRYSTALLIZATION. CRIOCRYSTALLOGRAPHY. CRYOPROTECTORS. (6 H LECTURE + 6 H LABORATORY)
DATA COLLECTION. RADIATION AND MATTER. X-RAY DIFFRACTION. X-RAY SOURCES: X-RAY TUBES AND SYNCHRTRON LIGHT. X-RAY DETECTORS: CCD AND IMAGE PLATE.ROTATING CRYSTAL METHOD. (6 H LECTURE + 3 H LABORATORY)
HOW TO SOLVE THE STRUCTURE: THE PHASE PROBLEM. STRUCTURE FACTOR AND ELECTRON DENSITY. HEAVY ATOM METHOD, SIR, MIR, MOLECULAR REPLACEMENT, SAD, MAD. ELECTRON DENSITY MAPS. CRYSTALLOGRAPHIC DISAGREEMENT INDICES. (4 H LECTURE + 3 H LABORATORY)
CRYSTALLOGRAPHIC DATABASES. PROTEIN DATA BANK. CARTESIAN COORDINATES AND CRYSTALLOGRAPHIC COORDINATES. PDB FILES. PROGRAMS FOR THE VISUALIZATION OF CRYSTAL STRUCTURES. (4 H LECTURE + 3 H LABORATORY)
ELECTRON MICROSCOPY AND ELECTRON DIFFRACTION. (4 H LECTURE + 3 H LABORATORY)

THE TOPICS ADDRESSED IN MODULE B ARE:
GENERAL PRINCIPLES OF SPECTROSCOPY. NUCLEAR MAGNETIC RESONANCE., 1H-NMR AND 13C-NMR AND MULTIPULSE MULTIDIMENSIONAL NMR TECHNIQUES (12H LECTURE, 10H LABORATORY). MASS SPECTROMETRY: INTRODUCTION, IONISATION PROCESSES, FRAGMENTATION PROCESSES (8H LECTURE, 6H LABORATORY), APPLICATIONS. ULTRAVIOLET AND VISIBLE SPECTROSCOPY: MOLECULAR ORBITAL AND ELECTRONIC TRANSITIONS, CHROMOPHORES,APPLICATIONS (6H LECTURE, 4H LABORATORY). INFRARED SPECTROSCOPY, MOLECULAR VIBRATIONS ,STRUCTURAL INFORMATIONS IN MACROMOLECULES WITH VIBRATIONAL SPECTROSCOPY (6H LECTURE, 3H LABORATORY).

	Teaching Methods
	THE TEACHING COURSE CONSISTS OF 56 HRS: 32 HOURS (4 CFUS) ARE DEVOTED TO LECTURES AND 24 HOURS (2 CFUS) TO PRACTICAL SESSIONS. DURING THE LECTURES SLIDE PRESENTATIONS ARE USED TOGETHER WITH MULTIMEDIA MATERIAL VIA THE WEB. DURING THE PRACTICAL SESSIONS EACH STUDENT CARRIES OUT EXPERIMENTS RELATED TO THE STRUCTURAL CHARACTERIZATION OF A PROTEIN, AS CRISTALLIZATION, STRUCTURAL DETERMINATION AND VALIDATION.

Teaching Methods

THE TEACHING COURSE CONSISTS OF 56 HRS: 32 HOURS (4 CFUS) ARE DEVOTED TO LECTURES AND 24 HOURS (2 CFUS) TO PRACTICAL SESSIONS.
DURING THE LECTURES SLIDE PRESENTATIONS ARE USED TOGETHER WITH MULTIMEDIA MATERIAL VIA THE WEB.

DURING THE PRACTICAL SESSIONS EACH STUDENT CARRIES OUT EXPERIMENTS RELATED TO THE STRUCTURAL CHARACTERIZATION OF A PROTEIN, AS CRISTALLIZATION, STRUCTURAL DETERMINATION AND VALIDATION.

	Verification of learning
	THE EXAM CONSISTS OF A DETAILED DESCRIPTION OF A 3D PROTEIN STRUCTURE CHOSEN BY THE STUDENT USING THE PROTEIN DATA BANK. STUDENTS ARE INVITED TO PRESENT A SLIDE SHOW, WHICH IS USED A STARTING POINT TO DISCUSS THE MAIN TOPICS OF THE TEACHING PROGRAM. THE FINAL ASSESSMENT TAKES INTO ACCOUNT THE DEGREE OF UNDERSTANDING OF THE STUDENT, THE EXACTNESS OF THE USED TERMS, CRITICAL THINKING AND ABILITY TO CREATE AND UNDERSTAND CONNECTIONS BETWEEN THE VARIOUS TOPICS THE EXAM AIMS TO ASCERTAIN THE KNOWLEDGE AND THE UNDERSTANDING OF THE COURSE CONTENTS, THE ABILITY TO APPLY THE ACQUIRED SKILLS AND TO DEVELOP INDEPENDENT SOLUTIONS.

Verification of learning

THE EXAM CONSISTS OF A DETAILED DESCRIPTION OF A 3D PROTEIN STRUCTURE CHOSEN BY THE STUDENT USING THE PROTEIN DATA BANK.
STUDENTS ARE INVITED TO PRESENT A SLIDE SHOW, WHICH IS USED A STARTING POINT TO DISCUSS THE MAIN TOPICS OF THE TEACHING PROGRAM.
THE FINAL ASSESSMENT TAKES INTO ACCOUNT THE DEGREE OF UNDERSTANDING OF THE STUDENT, THE EXACTNESS OF THE USED TERMS, CRITICAL THINKING AND ABILITY TO CREATE AND UNDERSTAND CONNECTIONS BETWEEN THE VARIOUS TOPICS
THE EXAM AIMS TO ASCERTAIN THE KNOWLEDGE AND THE UNDERSTANDING OF THE COURSE CONTENTS, THE ABILITY TO APPLY THE ACQUIRED SKILLS AND TO DEVELOP INDEPENDENT SOLUTIONS.

	Texts
	A. IMMIRZI, C. TEDESCO LA DIFFRAZIONE DEI CRISTALLI, LIBRERIAUNIVERSITARIA.IT EDIZIONI, 2017. A. DUCRUIX, R. GIEGE' CRYSTALLYZATION OF NUCLEIC ACIDS AND PROTEINS A PRACTICAL APPROACH, OXFORD UNIVERSITY PRESS

	More Information
	THE COURSE NOTES ARE MADE AVAILABLE ON THE WEBSITE AND WITHIN MICROSOFT TEAMS. https://docenti.unisa.it/004461/risorse?categoria=335&risorsa=1139 https://unisalerno.sharepoint.com/sites/StrutturisticaBiomolecolare/Materiale%20del%20corso/Forms/AllItems.aspx

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