Degree | Type | Year | Semester |
---|---|---|---|
4313794 Biochemistry, Molecular Biology and Biomedicine | OT | 0 | 1 |
University degree in Biochemistry, Biotechnology, Biology, Biomedical Sciences, Genètica, Microbiology, Chemistry, Informatics, Phisics, Veterinary, Pharmacy or Medicine.
-The main goal of the course is to introduce the different biophysical methods used in Biomedical research. The student will acquire the knowledge to understand of the techniques utilized to study the structure and function of macromolecules (proteins, nucleic acids, sugars, macromolecular complexes), according to the state of the art of this techniques in relation to biomedical applications.
-A major objective is to acquire the basic knowledge to solve three-dimensional structures of proteins and their complexes by X-ray crystallography by means of a sincrotron light source. At the end of the course the student will know the theoretical and practical methods to solve three-dimensional structures of proteins, including protein crystalllization in the laboratory and the resolution of protein structures by means of bioinformatics tools.
- At the end of the course the student will know the basic experimental and thoretical methodology to study the properties of macromolecules.
- Structural dynamics.
- Circular dichroism (CD)
-Dynamic Light Scattering (DLS) (Theory and practical course)
-Interactomics: Basis for protein interactions, at the binary or massive level.
- Structural analysis by Nuclear Magnetic Ressonance.
- Aplications of syncrotron radiation in Biomedicine.
- Structural characteritzation of peptides and proteins related to degenerative precesses and viral infection.
- Immunotherapy with antibiotic fragment: CD, FTIR and fluorescence techniques application to protein design.
- Study of Intrinsically Disordered Proteins
- Structure, dynamics and topology of DNA. Biomedical aspects.
- Analysis of macromolecules complexes and biomolecule interactions using microscopical techniques
- Introduction and practical course to prepare protein crystals
- Visit to the protein crystallography beamline at the ALBA syncrotron.
- Practical computational course to solve protein structures
- The working methodology combines theoretical lectures with autonomous work by the student. There will be computer courses and also an initial cristallography course in the laboratory. The course pretends to be more practical. There will also be a visit at the ALBA synctrotron, particularly at the X-ray diffraction for protein crystallography.
Annotation: Within the schedule set by the centre or degree programme, 15 minutes of one class will be reserved for students to evaluate their lecturers and their courses or modules through questionnaires.
Title | Hours | ECTS | Learning Outcomes |
---|---|---|---|
Type: Directed | |||
Knowledge of biophysical methods and identification of biomolecules properties | 70 | 2.8 | 2, 10, 6, 7 |
Type: Supervised | |||
X-ray data processing and protein model building with computers | 35 | 1.4 | 8, 9, 11 |
Type: Autonomous | |||
New idea development in research and critical arguing | 52 | 2.08 | 1, 5, 4, 13 |
Scientific communication | 30 | 1.2 | 3, 15 |
use of acquired knowledge | 35 | 1.4 | 12, 16, 14 |
- In the final evaluation it will be considered the assistance (which is mandatory), the involvement in the lectures, and a short test held on the last day of the module based on the main topics of the course.
- "Non evaluable" will be considered when the evaluation activities (final test and assistance) will not reach a minimal qualification of 5,0.
Important: If plagiarism is detected in any of the works submitted, the student will fail the whole module.
Final mark = T* 0,50 + Av* 0,3 + PC* 0,2
T (Final exam)
Av (continued evaluation)
PC (contribution in classes)
There will be a retake examination possibility. To be eligible for the retake process, the student should have been previously evaluated in a set of activities equaling at least two thirds of the final score of the course or module. Thus, the student will be graded as "No Avaluable" if the weighthin of all conducted evaluation activities is less than 67% of the final score
Title | Weighting | Hours | ECTS | Learning Outcomes |
---|---|---|---|---|
Active student involvement | 20 | 0 | 0 | 5, 12, 3, 4, 13, 15 |
Continued evaluation | 30 | 1.12 | 0.04 | 1, 2, 10, 6, 7, 8, 9, 11, 16, 14 |
Writing of test evaluation | 50 | 1.88 | 0.07 | 1, 2, 10, 6, 7, 8, 9, 11, 16, 14 |
- Each lecturer will provide particular bibliography corresponding to their specific topics.
ebook:
Integrative structural biology with hybrid methods / Haruki Nakamura, Gerard Kleywegt, Stephen K. Burley, John L. Markley, editors. Llibre en línia | 2018
Links:
http://www-structmed.cimr.cam.ac.uk/course.html
http://www.xtal.iqfr.csic.es/Cristalografia/index-en.html
UCSF Chimera; VMD; CCP4 interfase package; Coot; Phenix; Pymol.