CLIL

1. CLIL WhatisCLIL? WhyCLIL?

2. C ontents and Language Integrated L earning ……….... ………….. …………………. ………… …….

3. Goalstobeachieved: • The Four C’s: Content, Communication, Cognition, Culture • CLILenablesstudentstolearnaboutvarioussubjectsastheylistento, talk about, readabout, and writeabout the content in a secondlanguage • CLILincorporatessubject-specificachademicvocabulary in lessonsvehicolated in a secondlanguage • Studentsacquirelistening, speaking, reading, writingskills in content and languageintegratedinstruction

4. CLILlinks • https://youtu.be/uIRZWn7-x2Y • https://youtu.be/7QOPHRHJvPc • https://youtu.be/ssPbrPpuXbI

5. OurCLILEperience School: Liceo Scientifico “A. Scacchi” Class: 5^ I 2018-19 VehicularLanguage: English Subject : Chemistry Topic : Biomolecules Contents: Amino acids and Proteins Teachers : Vincenza Manodoro Elisabetta Casamassima

6. Amino Acids and Proteins Biomoleculescontainingspecificchemicalelements: Carbon (C) Hydrogen(H) Oxygen (O) Nitrogen (N) Sulfur (S) (smallquantities) • Amino acids: 20 smallmoleculesjoinedtoghetherend-to end in long chains in anyorder, tomake a proteinmolecule. • Eachproteinismadeofmoleculeswithamino acids in a precise order

7. Basic Structure of an Amino Acid Functionalgroups: - NH2α - amino group (basic) - COOH - carboxylgroup (acidic) - Cα - carbon - R R- group or side-chain - H α - hydrogen H H2N– C – COOH R https://youtu.be/J6R8zDAl_vw

8. Amino Acids: isoelectricpoint and zwitterions • The isoelectric point of an amino acid is the pH at which the amino acid has a neutral charge • You will learn how to calculate the isoelectric point, and the effects of pH on the amino acid's overall charge • We will also discuss zwitterions, or the forms of amino acids that dominate at the isoelectric point https://www.youtube.com/watch?v=42llTiRn-b8

9. From Amino AcidstoProteins • Proteins are made up froma long chainof amino acid subunitsjoinedtogetherby a condensationpolymerisation • Whenmonomersreacttogether, anamide-linkage (or peptide linkage) isformedtoproduce a dipeptide • Whenthisisrepeatedmanytimes, a polymerisformed. Short polymers(up to 15 amino acids) are knownaspolypeptides. Chainsinvolvingmore than 100 amino acidsare calledproteins https://youtu.be/EweuU2fEgjw

10. FourlevelsofProteinstructure - 1 • Primary structure The simplest level of protein structure, primary structure, is simply the sequence of amino acids in a polypeptide chain.  Each chain has its own set of amino acids, assembled in a particular order. The sequence of the chain starts at the N-terminus and ends at the C-terminus. Even changing just one amino acid in a protein’s sequence can affect the protein’s overall structure and function. For instance, a single amino acid change is associated with sickle cell anemia: the glutamic acid that is normally the sixth amino acid of the hemoglobin β chain is replaced by a valine. A personwhose body makesonlysicklecellhemoglobinwillsuffersymptomsofsicklecell anemia. Theseoccurbecause the glutamicacid-to-valine amino acid changemakes the hemoglobinmoleculesassembleinto long fibers

11. FourlevelsofProteinstructure - 2 • Secondary structure The next level of protein structure, secondary structure, refers to local folded structures that form within a polypeptide due to interactions between atoms of the backbone. (The secondary structure does not involve R group atoms.) The most common types of secondary structures are the α helix and the β pleated sheet. Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another

12. FourlevelsofProteinstructure - 3 • Tertiary structure The overall three-dimensional structure of a polypeptide is called its tertiary structure. The tertiary structure is primarily due to interactions between the R groups of the amino acids that make up the protein. R group interactions that contribute to tertiary structure include hydrogen bonding, ionic bonding, dipole-dipole interactions, and London dispersion forces – basically, the whole gamut of non-covalent bonds. Finally, there’s one special type of covalent bond that can contribute to tertiary structure: the disulfide bond. Disulfide bonds, covalent linkages between the sulfur-containing side chains of cysteines, are much stronger than the other types of bonds that contribute to tertiary structure. They act like molecular "safety pins" keeping parts of the polypeptide firmly attached to one another.

13. FourLevelsofProteinStructure - 4 • Quaternary structure Many proteins are made up of a single polypeptide chain and have only three levels of structure (the ones we’ve just discussed). However, some proteins are made up of multiple polypeptide chains, also known as subunits. When these subunits come together, they give the protein its quaternary structure. https://youtu.be/EweuU2fEgjw

14. ProteinFunctions in Humans • Manyfunctions, including: https://www.youtube.com/watch?v=qBRFIMcxZNM • Catalysts (enzymes) https://www.youtube.com/watch?v=-VrtBFZa5TE • Transportmolecules(e.g. haemoglobin) * https://www.youtube.com/watch?v=WXOBJEXxNEo • Structuralmaterials(e.g. in muscles) https://www.youtube.com/watch?v=qwnySVtllTA • Hormones (e.g. insulin)https://www.youtube.com/watch?v=cHrFyFZCHeI • Storage(e.g. ferritin) https://www.youtube.com/watch?v=NvNINrtE39g • Defenceagainstdesease(e.g. antibodies) https://www.youtube.com/watch?v=68T-QUIEp_o • MolecularChaperones

15. ProteinFunction and Shape • Proteindenaturation and Denaturatingfactors https://www.youtube.com/watch?v=dNHtdiVjQbM • Renaturatedproteinsand MolecularChaperones https://www.youtube.com/watch?v=d1QIEQEyYRo

16. Proteinmodifications • Co-traslationalmodifications(e.g. acetylation) • Post-traslationalmodifications(e.g. glycosylation) • Phosphorylation • Methylation • Proteolysis • Ubiquitination https://www.youtube.com/watch?v=K2bGjTaNsnM