Teaching GuideTerm
Faculty of Science
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Grao en Bioloxía
 Subjects
  Biochemistry I
   Contents
Topic Sub-topic
SECTION 1. INTRODUCTION TO BIOCHEMISTRY 1. Biochemistry, origins and evolution until the present
2. Biomolecules and Bioelements:Concept. Origins and Evolution of Biomolecules
3. Review of functional groups, chemical bonds and stereochemistry
4. Biomolecules in its aqueous environment
SECTIION 2. BIOCHEMISTRY METHODOLOGY 1. General aspects of biochemistry methodology
2. Biological material used in biochemistry
3. Techniques tissue homogenate. Fractionation of cellular organelles
4. Fractional precipitation and centrifugation
5. Chromatographic techniques
6. Electrophoretic techniques
7. Dialysis and ultrafiltration
8. Radioactivity and isotopic techniques in biochemistry
9. Spectroscopic techniques
SECTION 3. CARBOHYDRATES Monosaccharides
1. Concept, classification and biological importance of carbohydrates
2. Configuration, conformation and cyclic structure of monosaccharides
3. Physical and chemical properties
4. Most important derivatives: structure and function

Oligosaccharides and polysaccharides
1. Properties of the O-glycosidic bond
2. Nomenclature, classification, structure, properties and biological significance of most important oligosaccharides
3. Analysis and identification techniques
4. Polysaccharides: concept and classification
5. Most important glucans: structure and biological function
SECTION 4. LIPIDS Fatty acids, glycerides and glycerides
1. Concepts, classification and biological importance
2. Fatty Acids. General characteristics. Classification and nomenclature. Physical and chemical properties
3. Isolation and identification techniques
4. Fatty acid derivatives: Prostaglandins, thromboxanes and leukotrienes
5. Waxes. Definition, structure and biological function
6. Glycerides. Definition, structure and nomenclature. Properties and structural analysis

Phosphoglycerides and sphingolipids. Terpenes and steroids
1. Phosphoglycerides. Structure and classification. Properties and biological function
2. Sphingolipids: Phosphosphingolipids and glycosphingolipids. Structural analysis. Phospholipids and biological membranes
3. Terpenes. Structure, classification and nomenclature. Biological functions
4. Steroids. Structure, classification and nomenclature. Sterols, bile salts and steroid hormones: biological functions

Pyrrolic lipids
1. The pyrrole ring
2. Pirrolinic compounds: linear and cyclic pyrroles
3. Pyrrole compounds as members of conjugated proteins
4. Porphyrias and other pathologies
SECTION 5. AMINOACIDS, PEPTIDES AND PROTEINS Amino acids: properties and purification
1. Structure, stereochemistry and classification of amino acid building blocks of proteins
2. Other amino acids
3. Physical and chemical properties of amino acids
4. Chemical reactivity of the amino acids
5. Purification and identification of amino acids

Primary structure of peptides and proteins
1. The peptide bond and its features. The amide bond. Physical and chemical properties of the peptides.
2. Nomenclature of peptides. Peptides of biological interest
3. Proteins: general characteristics. Concept. Classification criteria. Physical and chemical general properties
4. Structure levels of proteins
5. Primary structure of proteins. Concept of primary structure. Types of proteins according to their primary sequence

Secondary structure of proteins
1. Linus Pauling and Robert Corey. Concept of secondary structure
2. Alpha helix, beta sheets, and beta turns. Regions without secondary structure: Structural Features.
3. Prediction of secondary structures: Statistical methods
4. Stabilization of secondary structures

Spatial conformation of proteins
1. Concept of tertiary structure, supersecondary structure and domain
2. Stability of the three dimensional structure of proteins
3. Fibrous and globular proteins: characteristics and content in secondary and supersecondary structures and domains
4. Characteristics of protein folding
5. Quaternary structure of proteins

Protein properties. Extraction, purification and characterization
1. Physical properties. Denaturation and renaturation concepts: causes and effects. Protein absorbance at 280 nm
2. Chemical properties. Amphoteric character of proteins. Reactivity of the side chains of amino acids
3. Methods for determining protein concentrations
4. Methods of extraction, separation, purification and concentration of proteins
5. Methods for protein characterization: molecular weight, pI and number of monomers

Structural analysis of the proteins
1. Analysis of the primary structure. Analysis of amino acid composition and identification of the amino terminal residue
2. Automated sequencing of a short polypeptide: Edman degradation
3. Sequencing and automated protein synthesis
4. Localization of modified amino acid by mass spectrometry
5. Analysis of the secondary structures: circular dichroism
6. Analysis of the tertiary structure: X-ray diffraction and nuclear magnetic resonance

Conjugated proteins
1. Concept and types
2. Collagen
3. Hemeproteins: Types and structural and functional characteristics
4. Myoglobin and hemoglobin

Motor proteins and antibodies
1. Actin and myosin. General and structural characteristics
2. The Muscle contraction
3. General structure of immunoglobulins
SECTION 6. NUCLEOTIDES AND NUCLEIC ACIDS

Nucleotides
1. Nucleotides: definition, composition and general structure
2. Physical and chemical properties of bases
3. Important functional groups of the bases
4. Nucleotides as structural components of nucleic acids: phosphodiester bond
5. Nucleotides with other biological functions
6. Natural modifications and mutation of the bases

Deoxyribonucleic and ribonucleic acids
1. Definition and general characteristics of nucleic acids
2. Compositional and structural differences between DNA and RNA
3. Deoxyribonucleic acids: The DNA double helix and the tertiary structures of DNA. Structural characteristics of the different types of genomes
4. DNA sequencing techniques: The Sanger method
5. Ribonucleic Acids: François Jacob and Jacques Monod: theory of the information transport from DNA to protein. Types of RNA: function and structure

Properties and characterization of DNA and RNA
1. Denaturing agents: related to the temperature and pH
2. Loss of secondary and tertiary structure of nucleic acids: consequences
3. The Tm (melting temperature) and its relation to the length and nucleotide composition of the nucleic acids
4. Kinetics and monitorization of the denaturation-renaturation process: the hyperchromic effect of the denaturation
5. Hybridization concept: formation of pure and hybrid duplexes. Techniques: Southern and Northern blot
SECTION 7. PRINCIPLES OF BIOENERGETICS 1. Review of the thermodynamics principles applied to biological systems
2. Concept of coupled reaction and ATP cycle
3. Energy carrier molecules
4. Electron transporter molecules
5. Acetyl groups transporter molecules
SECTION 8. ENZYMOLOGY

Enzymes as biological catalysts
1. General characteristics and biological function
2. Advantages of enzymes over chemical catalysts
3. Classification of enzymes
4. Reactions catalyzed by different classes of enzymes
5. Cofactors, coenzymes and role of vitamins
6. Principal reactions where the coenzymes are involved

Action mechanisms of the enzymes
1. Role of enzymes in biological reactions and metabolism
2. Speed of reactions and activation energy
3. Enzymes from the structural viewpoint. The active site: three dimensional structure and substrate recognition capability. Side chains of amino acids and catalysis
4. Models that explain the activation energy decrease in the enzymatic reaction
5. Review of heterolithic and homolithic reactions. Nucleophilic and electrophilic reagents
6. Other molecules as biological catalysts: Antibodies as catalysts (abzymes), ribozymes, DNAzymes and Sinzymes
7. Enzymes used in clinical analysis, in the diagnostic of diseases, or as therapeutic agents
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