PROTEINSBuilding blocks of proteins: Amino Acids (Generally 20 amino acids)Each amino acid consists of a central carbon atom bonded to four covalent partnersThese attachment groups are common to all amino acids:A carboxyl group (-COOH)An amino group (-NH2)A hydrogen atomA unique R groupTo make a polymer attach the OH of the carboxyl group and the H of the aminogroup removing them through the dehydration reactionAverage size of a protein molecule: 300 amino acidsProtein functions are influenced by there three-dimensional structure. They have tobe folded in a very specific wayPrimary Structure: Unique sequence of amino acids arranged in a long chainSecondary Structure: Affected by pattern of hydrogen bonds between amino acids in a long chain. When it starts folding (Slinky)Alfa helix and B pleated sheetsTertiary Structure: Dictated by primary and secondary structure. Folding leading to 3D shape (Globules shape)Quaternary Structure: Made up of several polypeptide chains that must fit together to form functional protein. Four Tertiary structures are put together. (ex. Hemoglobin)Denaturation: When an unfavorable change in temperature and/or PH, it canunravel the protein and cause it to lose its shape. (High fever above 104F)Enzymes (E)Protein molecules that act as catalystsReact with specific substances called substrates (S)3D structure of active site is critical to binding of E to SInhibitors – Decreases reaction rateProtein Misfolding and DiseaseMisfolded proteins are associated with for:Alzheimer’sMad CowParkinson’sSickle cell anemiaCystic fibrosisProteins go into a “Cage” and a Chaperonin or “lid” will seal it in to protect the protein while it folds then it is releasedNUCLEIC ACIDSFunction: Information storage (DNA and RNA)A gene is a specific stretch of DNA that programs the amino acid sequence of aPolypeptide.The chemical code of DNA must be translated from “nucleic acid language” to“Protein language”This is done through the RNA.Nucleic Acids are polymers made from monomers called nucleotidesEach nucleotide has three partsA five-carbon sugarA phosphate groupNitrogen – containing base (A, G, C, T)Dehydration reactions link nucleotide monomers into long chains calledpolynucleotides. They form covalent bonds between the sugars of one nucleotideand the phosphate of the next and form sugar-phosphate backbones.BIOl-L 112 1st Edition Lecture 3Outline of Last Lecture II. Four types of macromolecules A. Chart on function and components B. Chemistry of life III. Carbohydrates a. Functions in plants and animals b. Structure and function imagec. Types of Carbohydrates IV. Fats a. Functions b. Structure c. Types of Fats Outline of Current Lecture V. Proteins a. Make up of a protein b. Structures c. DenaturationVI. Nucleic Acids a. Make up of Nucleic Acids b. Dehydration Reactions Current LectureThese 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. PROTEINS Building blocks of proteins: Amino Acids (Generally 20 amino acids) Each amino acid consists of a central carbon atom bonded to four covalent partners These attachment groups are common to all amino acids: A carboxyl group (-COOH)An amino group (-NH2) A hydrogen atom A unique R group To make a polymer attach the OH of the carboxyl group and the H of the aminogroup removing them through the dehydration reaction Average size of a protein molecule: 300 amino acids Protein functions are influenced by there three-dimensional structure. They have to be folded in a very specific way o Primary Structure: Unique sequence of amino acids arranged in a long chain o Secondary Structure: Affected by pattern of hydrogen bonds between amino acids in a long chain. When it starts folding (Slinky)  Alfa helix and B pleated sheets o Tertiary Structure: Dictated by primary and secondary structure. Folding leading to 3D shape (Globules shape) o Quaternary Structure: Made up of several polypeptide chains that must fit together to form functional protein. Four Tertiary structures are put together. (ex. Hemoglobin)Denaturation: When an unfavorable change in temperature and/or PH, it can unravel the protein and cause it to lose its shape. (High fever above 104F) Enzymes (E) Protein molecules that act as catalysts React with specific substances called substrates (S) 3D structure of active site is critical to binding of E to S Inhibitors – Decreases reaction rate Protein Misfolding and Disease Misfolded proteins are associated with for:  Alzheimer’s  Mad Cow  Parkinson’s  Sickle cell anemia  Cystic fibrosis Proteins go into a “Cage” and a Chaperonin or “lid” will seal it in to protect the protein while it folds then it is released NUCLEIC ACIDS Function: Information storage (DNA and RNA) A gene is a specific stretch of DNA that programs the amino acid sequence of a Polypeptide. The chemical code of DNA must be translated from “nucleic acid language” to “Protein language”This is done through the RNA.Nucleic Acids are polymers made from monomers called nucleotides Each nucleotide has three parts A five-carbon sugar A phosphate group Nitrogen – containing base (A, G, C, T) Dehydration reactions link nucleotide monomers into long chains called polynucleotides. They form covalent bonds between the sugars of one nucleotide and the phosphate of the next and form sugar-phosphate