BIOLOGY 111 1st EditionLecture 6Outline of Last Lecture I. Functional GroupsII. Four major BiomoleculesIII. Dehydration and Hydrolysis ReactionsIV. CarbohydratesV. LipidsVI. ProteinsOutline of Current Lecture I. PolypeptidesII. Proteins structureA. Primary B. SecondaryC. TertiaryD. QuaternaryIII. Nucleic AcidsA. NucleotidesB. PolynucleotidesC. Chargaff’s ruleCurrent Lecture:Polypeptidepeptide bonds connect amino acids by dehydration (lose one water molecule)- N-terminus- C-terminusProteins are always in 3D *spherical (globular- round in shape) or *fibrous (ribbon-like and found mostly in muscles) ex. collagen... part of our body's framework (bones)1. protein structure (more complex)A. primary - single chain of amino acids (provides structure coding for how a protein will be made)B. secondary - interactions (backbone) of polypeptides causing coils or folding, repeated structurea. alpha helix (looks like a ribbon) These 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.b. beta pleated sheet (looks like jagged sheets) *need H with a partial charge to make bonds and hold secondarystructure (alpha and/or beta) togetherC. tertiary (most common) - gives 3D shape and contains a combination of alpha helix and beta sheeta. R group is very important because they form a variety of bonds... which stabilize the tertiary structure1. hydrogen bonds2. hydrophobic and Van der Waals interactions (asymmetrical charges)3. Disulfide Bridge (occurs when have sulfur)4. Ionic bonds D. quaternary - only formed when there are 2 or more polypeptides [ex.hemoglobin (4 polypeptides + ) and collagen...]*changing any part of any structure will result in a change throughout the stages afterex. if you change the primary structure, expect a change in the secondary, tertiary and quaternaryex. would be Red blood cell shape can be changed by replacing only one glu with valine and will result in sickled red blood cell this causes problems like anemia because they don't have enough oxygen flowing in their blood*may always affect secondary or tertiary but not necessarily always affect quaternary - unfolded, or denatured, proteins lose their normal properties BUT some proteins can successfully refold and renature- salt concentration, water content, temperature... affect the function of protein denatured proteins do not function like a normal proteinchaperonins - when protein folding takes a structure, it is done naturally and no outside help, it protects the protein while it is being folded from improper interactions (like going into a beauty parlor and coming out looking like a new person...) it is a protein itself so made up of amino acids Nucleic AcidsGenes are made of DNA, a nucleic acidthe amino acid sequence of a polypeptide is programmed DNA (one type) and RNA (variety of types) are polynucleotides which store and process info• Nucleotides - nucleic acid polynucleotide monomer• polynucleotide - held together by phosphate bonds• Pyrimidines (C, T, U)• Purines (A, G)Phosphate bonds (phosphodiester bonds) - hold nucleotides together between the sugars Chargaff's rule (A=T and G=C) complementary base pairing (by 5' end and 3' end)ex. hydrogen bonding between nitrogenous bases*in RNA (A=U and G=C) Test 1 ends here!- 40 questions (41 including bonus)- mostly multiple