In Biochemistry I, students will acquire basic knowledge of the molecular structures and functions making up living organisms. They will also develop essential laboratory skills to conduct simple biochemical experiments, and learn how to accurately describe, analyze, and critically interpret their findings.



Biochemistry I is a critical subject that, along with Biochemistry II, lays the groundwork for many of the subsequent courses in this field. It provides students with a strong foundation in the basic principles of biochemistry, which are essential to understand complex topics in the future.

COMPETENCIES / LEARNING OUTCOMES



Cross-cutting skills:



· Develop the ability for analysis, synthesis and critical reasoning in the application of the scientific method.



· Develop autonomous learning and adaptation to new situations.



· Develop ethical commitment and the ability to participate in social debate.



Specific skills:



· Acquire structural and functional knowledge of the molecules making up living beings, including their basic components and polymeric structures.



· Recognize the structures of different types of biomolecules.



· Understand the fundamentals of enzymatic reactions, including the concepts of catalysis, kinetics, and enzymatic inhibition.



· Apply acquired knowledge to solve qualitative and quantitative problems.



· Develop basic laboratory skills required to conduct simple biochemical experiments.

Theoretical and practical contents



Syllabus:



Topic 1. Concept of biochemistry. Its historical evolution. Place of Biochemistry among the experimental sciences. Objectives of Biochemistry.



Topic 2. Bioelements and biomolecules. Functional groups and bonds. Three-dimensional structure of biomolecules: isomerism and stereospecificity. Configuration and conformation.



Topic 3. Water as a solvent. Colligative properties. pH and buffers. Buffers of biological interest.



Topic 4. Proteins. Amino acids. The peptide bond. Peptides: structure and properties. Structural levels in proteins. Protein sequencing. Native structure and denaturation. Protein functions. Basic concepts for protein purification. Purity criteria.



Topic 5. Enzymes. Nomenclature and classification. Catalysis: thermodynamic and kinetic aspects. Enzyme kinetics. Michaelis-Menten equation. Graphical determination of Vmax and Km. Units of enzyme activity. Enzyme inhibition and regulation. Concept and types of inhibition. Covalent modifications of enzymes. Allosteric enzymes.



Topic 6. Carbohydrates. Functions and classification. Simple monosaccharides and derivatives. Oligosaccharides. Polysaccharides.



Topic 7. Nucleic acids. Concept and biological interest. Pyrimidine and pyrimidine bases. Nucleosides and nucleotides. Polynucleotides: primary, secondary and tertiary structure. Nucleic acid sequencing. Free nucleotides with specific functions. Intermediates of cellular chemical energy, cofactors of enzymatic reactions, cellular communication.



Topic 8. RNA. Composition and structure. Types of RNA: heterogeneous nuclear, small nuclear, transfer, ribosomal, messenger, viral. Catalytic RNA.



Topic 9. DNA. Structure and properties. Levels of structuring: A, B and Z helices. DNA as genetic material. Chromatin structure. Optical properties of DNA: fusion and renaturation. DNA hybridization. DNA-RNA hybrids.



Topic 10. Lipids. Functions and classification. Saponifiable and non-saponifiable lipids.



Topic 11. Biological membranes. Lipid bilayers. Composition, structure and properties. Membrane proteins. Dynamics of components. Liposomes.



The theoretical content described above will be applied to solve exercises and problems in class, as well as in laboratory sessions. During these laboratory sessions, students will have the opportunity to apply the knowledge they have acquired and develop their practical skills in a supervised setting.



1st session. Learning the use of automatic pipettes, pH measurement and preparation of buffer solutions.



2nd session. Quantification of sugars and use of a sucrose standard curve.



3rd session. Quantification of sucrose in breakfast cereals.



4th session. Separation of macromolecules by Gel Filtration Chromatography.

Topics 1 to 11 outlined in the syllabus will be explained in detail during lectures (M).



In classroom practices (GA), students will solve qualitative and quantitative exercises and problems related to the concepts covered in the lectures. In seminars (S), students will work on solving a simple biochemical question using the techniques they have learned.



In the laboratory sessions, students will carry out the four practical activities described above. Attendance to the practical sessions is mandatory.



In computer practical session, students will use the Jmol program to visualize biomolecules, including their isomerism and their structural and functional variability.



The theoretical content described above will be applied to solve exercises and problems in class, as well as in laboratory sessions. During these laboratory sessions, students will have the opportunity to apply the knowledge they have acquired and develop their practical skills in a supervised setting.



1st session. Learning the use of automatic pipettes, pH measurement and preparation of buffer solutions.



2nd session. Quantification of sugars and use of a sucrose standard curve.



3rd session. Quantification of sucrose in breakfast cereals.



4th session. Separation of macromolecules by Gel Filtration Chromatography.

• Final Assessment System
• Tools and qualification percentages:
  • Realization of Practical Work (exercises, cases or problems) (%): 35
  • Team projects (problem solving, project design)) (%): 5
  • praktiken azterketa (garatu beharreko galderak eta ariketak) (%): 60

EVALUATION SYSTEM



Final evaluation system



QUALIFICATION TOOLS AND PERCENTAGES



· Practical sessions (exercises, problems…) 35%



· Teamwork (problem solving, Project design) 5%



· Written exam (multiple choice questions + short questions) 60%



ORDINARY ASSESSMENT SESSION: GUIDELINES AND OPTING OUTANCE



The assessment of the Biochemistry I course is divided into three sections:



a) 60% Written exam (multiple-choice questions and short questions).



b) 35% Laboratory, classroom and computer practical sessions (20% GL+10% GA+5% GO).



c) 5% Teamwork (problem solving, project design, etc).



The criteria for assessing the sections are as follows:



· Appropriateness of the answers, integration of information, approach to and development of the problem exercise, correct use of units of measurement, and clarity and precision of language.



· Adequate execution of the experimental protocol, analysis and interpretation of



results, and effective presentation of findings.



· Correct approach and execution of exercises, as well as thorough completion and presentation of assigned tasks.



The final grade for the course will be calculated by adding the partial grades of each assessed section. To pass the course and to have your overall grade calculated, you must obtain a minimum percentage of the maximum grade in each of the following sections:



a) Written test: 50%.



b) Laboratory practice test: 40%.



c) Classroom practice test: 30%.



Attendance to laboratory session is mandatory.



Waiving: Failing to take the final exam is sufficient to waive the final grade.



Not taking the final exam is enough to receive a grade of "not presented" for the course.



The use of books, notes, phones, electronic devices, computers, or other equipment is not allowed during assessment tests (except for a calculator*). If any academic dishonesty or fraudulent practices are detected, the protocol on academic ethics and prevention of such practices at UPV/EHU will be enforced.

EXTRAORDINARY ASSESSMENT SESSION: GUIDELINES AND OPTING OUT



The final grade will be calculated by adding the grades obtained in the following sections:



a) Written exam (multiple-choice test and short questions) (70%)



b) Laboratory sessions (20%)



c) Classroom practical sessions (10%)



The grades of the sections passed will be kept for the extraordinary assessment session of that school year (until July) if the subject is failed in the ordinary call. Neither the computer practices nor the seminars will be assessed in the extraordinary session; however, if these sections are passed in the ordinary session, those grades will be maintained for the extraordinary session and the corresponding percentage will be deducted from the written test.



The final grade of the course will be obtained by adding the grades of each assessed section. In order to pass the subject, and averaged with the other sections of the subject, the minimum percentage over the maximum grade must be obtained in the following sections:



a) Written test: 50%.



b) Laboratory practice test: 40%.



c) Classroom practice test: 30%.



Attendance of laboratory sessions is mandatory. Students that do not attend those laboratory sessions during the ordinary session, will not have another chance to do so during the extraordinary session.



Not taking the written test will be qualified as "not presented" in the final grade for the course.



The use of books, notes, phones, electronic devices, computers, or other equipment is not allowed during assessement tests (except for a calculator*). If any academic dishonesty or fraudulent practices are detected, the protocol on academic ethics and prevention of such practices at UPV/EHU will be enforced.

MATERIALS REQUIRED

The eGela webpage (http://egela.ehu.eus) will be used to publish the course guide and information about the activities performed in the laboratory, computer room and classroom.

Before entering the laboratory, students must carefully read the protocol for the corresponding session. This protocol will be uploaded to eGela.

Basic bibliography

RECOMMENDED READINGS



Basic bibliography



Lehninger Principles of Biochemistry, (2012) 6th Edition, Nelson D.L. & Cox. M. M., Freeman and Company, New York.



Bioquímica (2013) (6ª ed) Stryer L., Berg J. M. & Tymoczko J. L., Editorial Reverte, Barcelona.



Bioquímica curso básico (2014) Tymoczko J. L. , Berg J. M., Stryer L., Editorial Reverte, Barcelona



BIOQUÍMICA Las bases moleculares de la vida (2009) 4 Ed., McKee T. & McKee. J.R., McGraw Hill Interamericana Editores, México.

In-depth bibliography

In-depth bibliography

Molecular Biology of the Cell (2008) (5th ed) Alberts A., Johnson A., Lewis J., Raff M., Roberts K. & Walter P., Garland Science, New York.

Fundamentals of Biochemistry (2006) 2nd ed., Voet D., Voet J.G. & Pratt CW., John Wiley & Sons, New York.

Bioquímica (2002) 3ª edición, Mathews, C.K. & van Holde, K.E., McGraw Hill Interamericana, Madrid.

Journals

Journals

· Nature

· Science

· Investigación y Ciencia

Web addresses

http://www.biology.arizona.edu/default.html
http://wwwbioq.unizar.es/
http://www.zientzia.net
http://www.ehu.es/biomoleculas
http://www1.euskadi.net/euskalterm/indice