Studying at the University of Verona
Here you can find information on the organisational aspects of the Programme, lecture timetables, learning activities and useful contact details for your time at the University, from enrolment to graduation.
Study Plan
This information is intended exclusively for students already enrolled in this course.If you are a new student interested in enrolling, you can find information about the course of study on the course page:
Laurea magistrale in Molecular and Medical Biotechnology - Enrollment from 2025/2026The Study Plan includes all modules, teaching and learning activities that each student will need to undertake during their time at the University.
Please select your Study Plan based on your enrollment year.
1° Year
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2 courses to be chosen among the followingOne course to be chosen among the following3 courses to be chosen among the followingOne course to be chosen among the following2° Year activated in the A.Y. 2017/2018
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2 courses to be chosen among the following| Modules | Credits | TAF | SSD |
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2 courses to be chosen among the followingOne course to be chosen among the following3 courses to be chosen among the followingOne course to be chosen among the following| Modules | Credits | TAF | SSD |
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2 courses to be chosen among the followingLegend | Type of training activity (TTA)
TAF (Type of Educational Activity) All courses and activities are classified into different types of educational activities, indicated by a letter.
Structural biology (2016/2017)
Teaching code
4S003665
Teacher
Coordinator
Credits
6
Also offered in courses:
- Structural biology of the course Master's degree in Science and Technology of Bio and Nanomaterials (interuniversity)
Language
English
Scientific Disciplinary Sector (SSD)
BIO/11 - MOLECULAR BIOLOGY
Period
II sem. dal Mar 1, 2017 al Jun 9, 2017.
Learning outcomes
The goal of the Structural Biology course for the degree in Bioinformatics and Medical Biotechnology is to develop in the student the skills necessary to critically read and assess scientific papers in this branch of science, specially in crystallography since NMR is covered by another course.
After an introduction discussing the relative weight of the different techniques used to determine the three-dimensional structure of biomolecules, the course concentrates on the theory and practice of macromolecular crystallography.
The fundamentals of the theory of diffraction, the modern methods of data collection and the phase problem are covered in detail. In addition, papers selected from the current literature dealing with important biological structures are read and discussed
Program
Introduction. Structural Biology. The Protein Data Bank. Methods used to determine the three-dimensional structure of macromolecules. Crystallography, Nuclear Magnetic Resonance and Electron Microscopy. The role of Biocrystallography in Structural Biology.
The theory of X-ray diffraction. Geometry of an X-ray scattering experiment. Scattering of a single electron and an atom. The atomic scattering factor. Structure factor. The structure factor of atoms not located at the origin. The diffraction pattern of a one-dimensional array of atoms. X-ray diffraction from a three-dimensional array of atoms. The von Laue scattering conditions. The structure factor of a crystal. Fourier transforms. Convolutions and their use in the computation of structure factors. Bragg’s law of diffraction.
Properties of crystals. Symmetry. Symmetry elements. Space groups. Reciprocal lattice. Preparation of macromolecular crystals. Properties of protein crystals. The relationship between the crystal lattice and the reciprocal lattice. The Ewald sphere. Determination of the space group and of the number of molecules in the unit cell of a macromolecular crystal.
Determination of the molecular structure by X-ray crystallography. The phase problem. Steps in determining the structure of a macromolecule. X-ray sources. Data collection methods. Solving the phase problem. The method of multiple isomorphous replacement. The Patterson function. Treatment of errors. Computation of electron density maps. Molecular replacement. Other methods used to solve the phase problem.
Model building and refinement. Interpretation of the electron density maps. Building the model. Refinement methods. Assessing the model quality. The R factor. Ramachandran plots. Checking the stereochemistry.
Some important results of Biocrystallography. Using the Fourier difference synthesis to study the function of proteins. Conformational changes. Time resolved Biocrystallography. The importance of synchrotron radiation
Examination Methods
Oral exam
