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Presentation
Presentation
The Physical Biochemistry course addresses the physicochemical principles underlying the structure, properties, characterization, and stability of proteins, relating molecular structure to biological function. Particular emphasis is placed on the different levels of protein structural organization and on the interactions that determine their conformation and properties. The principles of protein separation and purification are covered, with emphasis on chromatographic techniques, including ion-exchange, size-exclusion, and affinity chromatography. Protein characterization includes methods for identification, quality control, and assessment of sample homogeneity, namely mass spectrometry, circular dichroism, and nuclear magnetic resonance. Techniques for determining molecular mass, such as sedimentation, size-exclusion chromatography, and electrophoresis, are also addressed. Finally, the principles of protein stability are explored using biocalorimetry (DSC and ITC).
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Class from course
Class from course
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Degree | Semesters | ECTS
Degree | Semesters | ECTS
Bachelor | Semestral | 4.5
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Year | Nature | Language
Year | Nature | Language
2 | Mandatory | Português
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Code
Code
ULHT2532-16915
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Prerequisites and corequisites
Prerequisites and corequisites
Not applicable
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Professional Internship
Professional Internship
Não
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Syllabus
Syllabus
Review of protein structural levels (Primary, Secondary, Tertiary and Quaternary structure) Protein separation 2.1 Basic principles of chromatography 2.2 Chromatographic techniques 2.3 Fractionation and clarification 2.4 Monitoring of protein purification Molecular mass determination 3.1 Mass spectrometry 3.2 Sedimentation 4. Techniques for protein sample quality control 4.1 Circular Dichroism (CD) 4.2 Nuclear Magnetic Resonance (NMR) 5. Protein Stability 5.1 Calorimetry 5.2 Fluorescence
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Objectives
Objectives
The Physical Biochemistry course aims to develop knowledge and skills concerning the principles and techniques used in the characterization of macromolecules, particularly proteins. The main techniques for protein purification and characterization are covered, including chromatographic methods, sedimentation, mass spectrometry, electrophoresis, and biocalorimetric techniques. By the end of the course, students should understand the basic principles underlying these techniques and be able to select and apply appropriate methodologies for the purification and biochemical characterization of proteins. In particular, they should be able to develop strategies to separate a protein of interest from a protein mixture, select appropriate experimental techniques for its characterization, determine its molecular mass, and assess its stability.
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Teaching methodologies
Teaching methodologies
The course content is delivered through multimedia presentations, using illustrative images and diagrams to facilitate the understanding and organization of the subject matter and to promote students' interest and participation. The teaching and learning process also includes practical exercises, enabling students to apply theoretical concepts to experimental situations. In addition, a study visit to a research centre is organized, providing students with direct contact with equipment and methodologies used in protein characterization and enabling them to understand their applications in different scientific fields.
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References
References
Buxbaum, E. (2025). Biophysical chemistry of proteins: An introduction to laboratory methods (2nd ed.). Springer. Sheehan, D. (2009). Physical biochemistry: Principles and applications (2nd ed.). John Wiley & Sons. Sun, S. F. (2004). Physical chemistry of macromolecules: Basic principles and issues (2nd ed.). John Wiley & Sons. Kalidas, C., & Sangaranarayanan, M. V. (2023). Biophysical chemistry: Techniques and applications. Springer.
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Assessment
Assessment
Descrição dos instrumentos de avaliação (individuais e de grupo) ¿ testes, trabalhos práticos, relatórios, projetos... respetivas datas de entrega/apresentação... e ponderação na nota final.
Exemplo:
Descrição
Data limite
Ponderação
Teste de avaliação
dd-mm-yyyy
60%
Relatório + Apresentação oral dd-mm-yyyy
40%
(...)
Ensino presencial com aulas teóricas e laboratoriais: As aulas teóricas são aulas magistrais de frequência voluntária seguindo o programa definido. As aulas laboratoriais são aulas tutoradas, orientadas por um docente, e de frequência obrigatória, destinadas a aplicar as técnicas e os princípios teóricos. Os requisitos para aproveitamento são os seguintes:
A. Avaliação contínua
Frequência obrigatória das aulas laboratoriais.
Classificação prática igual ou superior a 9,5 valores (avaliação contínua do desempenho dos alunos, 40% na classificação final).
2 frequências teóricas, média com ponderação de 60 % (classificação final igual ou superior a 9,5valores).
B. Exame final
Exame com 2 componentes prática (40%) e teórica (60%). Nota igual ou superior a 9,5 valores em cada componente.
Isenção de repetir uma das 2 componentes em caso de nota igual ou superior a 9,5 valores obtida para essa componente em avaliação contínua ou exame final anterior.
Teaching includes lectures and practical classes. The lectures (explaining the main concepts) are of facultative attendance, following the defined syllabus. Practical laboratory classes are mandatory and are carried out under the guidance and orientation of a Professor, in order for students to practice the techniques and its principles taught in the lectures.
Minimum requirement to pass:
A. Continuos evaluation
Attendance of practical classes. Laboratory minimum classification of 9.5 values ( corresponding to 40% of the final classification). 2 mid-term written exams, average with 60% weight (minimum final classification of 9.5 values ).
B. Final examination
Written examination with 2 components: practical (40%) and theoretical (60%). Minimum classification of 9.5 values in each component.
Students with a minimum classification of 9.5 values in one of the components in a previous evaluation (continuous or written evaluation) are exempted from repeating that part of the exam.
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Mobility
Mobility
Yes
