MCB 150 1st Edition Lecture 5Outline of Last Lecture I. Types of monosaccharidesa. Hexosesb. Triosesc. PentosesII. Polysaccharidesa. Celluloseb. Starchc. GlycogenOutline of Current Lecture III. Introduction to ProteinsIV. Amino Acid PropertiesV. Structuresa. Primaryb. Secondaryc. Tertiaryd. QuaternaryCurrent LectureIntroduction to Proteins:Proeomics: the study of protein and protein activity; we are the products of our proteins and our protein functions. Proteins make up the biggest portion in the composition of macromolecules in a cellUses of Protein:- Movement: Actin and Myosin in muscle tissues- Defense: Antibodies aid the immune system- Structure: Keratin in hair- Transport: Hemoglobin transports oxygen to tissues- Signaling: Glucagon signals blood sugar levels- Catalysis/regulation/metabolism: Largest roles of ProteinsThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.Most of our genetic information are used as blueprints to making proteinsAmino Acids: monomers of proteins; everyone has an amino group, a carboxyl group, and a hydrogen. Only difference is the side chain.Peptide bond: bond that forms between amino acids through the process of condensation. Condensation: Amino group of incoming with the carboxyl of the existing group. Molecule of water is lost and a covalent bond is formed.Amino Acid Properties:20 amino acids that are found in proteins- Their only difference is the R groups, giving each amino acid certain properties- Because there are so many, there can be a huge number of different amino acid sequences (ex. Tripeptide has 8,000 possibilities)- Most proteins contain more than 100 amino acidsClassifying amino acid R-groups:- Uncharged, polar- Uncharged, nonpolar- Positively charged (basic)- Negatively charged (acidic)Polar amino acids: all have an oxygen in the side chainsNonpolar amino acids: most side chains are carbon and hydrogenStructures:Proteins can be found in infinite numbers of 3D conformations- This confirmation is critical to the proteins function- If a protein is folded incorrectly, it can cause complications like Alzheimer’s Parkinson’s etcPrimary Structure (1⁰):- Linear sequence from NC- All proteins have a unique primary structureSecondary structure (2⁰):- First level of folding- Stabilized by hydrogen bonds in between the peptide linkages- Peptide backbone is polar. - Independent of R groups and found n most proteins- Coil form (α-helix) sheet formed (β-pleated)Tertiary structure (3⁰):- Folded 3D shape that is totally unique- Final confirmation of some proteins- Due to interactions between r groups with both each other and the backbone- Stabilized by:o H bonds between polar side chainso H bonds between hydrophilic side chains and backbone.o Ionic bond between an acidic and a basic amino acido Hydrophobic clustering of non-polar side chainso Van der Waals forceso Disulfide linkages Quaternary structure (4⁰):- Found in proteins with multiple subunits- Subunits can be the same (homodimer) or different