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Ap Bio: Macromolec.
| Question | Answer |
|---|---|
| Macromolecule | Lots of molecules bonded together |
| 4 Categories of Macromolecules | Carbs, Lipids, Proteins, and Nucleic Acid (DNA) |
| Molecules | Many Atoms bonded together |
| How do we build polymers? | Dehydration Synthesis |
| How do we break polymers into monomers? | Hydrolysis Reaction |
| Sugars | Monosaccharides have molecular formulas that are usually multiples of C(H2O)n |
| Most common monosaccharide | Glucose (C6H12O6) |
| Monosaccharides are classified by | The location of the carbonyl group - as aldose (for aldehyde carbonyl) or ketose (for ketone carbonyl). The number of carbons in the carbon skeleton. |
| Disaccharide | Formed when a dehydration synthesis (condensation) reaction joins two monosaccharides |
| Glycosidic Linkage | covalent bond between monosaccharides |
| Polysaccharides | The polymers of sugars that have storage and structural roles Storage - energy storage Structural - makes up part of the cellular structure |
| Starch | Storage polysaccharide of plants, consists entirely of glucose monomers (polymer of glucose) |
| Glycogen | Storage polysaccharide in animals (also a polymer of glucose) |
| Cellulose | Major component of the tough outer wall of plant cells. Like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ; difference is based on two ring forms for glucose - alpha (a) and beta (B) |
| Alpha vs. Beta Glucose | Stereoisomers of each other; demonstrates how a polymer's structure and function depend on what build them |
| Lipids | Diverse group of hydrophobic molecules; one class of large biological molecules that DO NOT form polymers. Hydrophobic because they consist mostly of hydrocarbons. (e.x. fats (triglycerides), phospholipids, and steroids). |
| Fats | Constructed from glycerol and three fatty acid tails. Glycerol is a three-carbon alcohol with a hydroxyl group attached to each carbon. Fatty acid tail consists of a carboxyl group attached to a long carbon skeleton. |
| Ester Linkage | Bond between glycerol and fatty acid tail |
| Triglyceride | Fat molecule with three fatty acid tails. |
| Saturated Fatty Acid Tails | maximum number of hydrogen atoms possible and no double bonds |
| Unsaturated Fatty Acid Tails | one or more double bonds; not maximum number of hydrogen atoms. |
| Saturated Fats | A triglyceride that has all saturated fatty acid tails |
| Unsaturated Fats | A triglyceride that has at least one unsaturated fatty acid tail |
| Saturated Fats at room temp | Solid; most animal fats are saturated |
| Unsaturated Fats at room temp | Liquids; plant fats and fish fats are usually unsaturated |
| Hydrogenation | Process of converting unsaturated fats to saturated fats by adding Hydrogen |
| Hydrogenating vegetable oils | Can create unsaturated fats to saturated fats by adding Hydrogen. These trans fats may contribute more than saturated fats to cardiovascular disease |
| Adipose Cells | Humans and animals store their fat here; they also cushion vital organs and insulate the body |
| Phospholipids | Two fatty acid tails and a phosphate group are attached to glycerol; the two fatty acid tails are hydrophobic, but the phosphate group and its attachments form a hydrophilic head |
| Steroids | lipids characterized by a carbon skeleton consisting of four fused rings; cholesterol, and important steroid, is a component in animal cell membranes |
| Proteins | Account for more than 50% of dry mass of most cells; functions include structural support, storage and transport, cellular communication, movement, and defense against foreign substances. |
| Enzymes | Type of protein that act as catalysts to speed up chemical reactions; they can perform their functions repeatedly, functioning as workhorses that carry out the processes of life |
| Polypeptides | polymers built from the same set of 20 amino acids (monomer); a protein consists of one or more polypeptides |
| Amino Acid Monomers | ALL amino acids are organic molecules with CARBOXYL and AMINO groups; amino acids differ in their properties due to differing side chains called R GROUPS |
| Parts of protein | N-terminus, central carbon, c-terminus, and r group |
| Peptide Bonds | between amino acids; can only form off the c-terminus |
| Polypeptide | polymer of amino acid monomers; range in length from a few to more than a thousand monomers; each polypeptide has a unique linear sequence of amino acids |
| Polypeptides | made from amino acids monomers but must fold to become functional |
| Functional Protein | Consists of ONE OR MORE polypeptides twisted, FOLDED, and coiled into a unique shape; the structure of amino acids determines a protein's three-dimensional structure; AMINO ACID ORDER DETERMINES STRUCTURE DETERMINES FUNCTION |
| Four Levels of Protein Structure | Primary, Secondary, Tertiary, Quaternary |
| Primary | # and unique arrangement of amino acids (polypeptide chain); NO FOLD YET |
| Secondary | interactions between carboxyl and amino acid groups (BACKBONE); ALPHA HELICES and BETA PLEATED SHEETS |
| Tertiary | interactions between R-Groups; this can be first stage for a functional protein (one polypeptide chain that has folded) |
| Quaternary | More than one polypeptide chain interacting (also a functional protein) |
| Tertiary Structure | 5 influences on the FOLDING and STABILIZING of the tertiary structure - R-GROUP INTERACTIONS |
| 5 influences on the FOLDING and STABILIZING | 1) hydrophilic interactions (polar/electrically charged): hydrophilic outside 2) Hydrophobic interactions (nonpolar): hydrophobic inside 3) Hydrogen Bonds (polar) 4) Ionic Bonds (electrically charged) 5) Disulfide Bridge (2 cysteine aa/crosslinking) |
| Quaternary Structure | Multiple polypeptide chains are put together; chains are held together/stabilized by the same interactions of the tertiary structure |
| 5 influences on quat structure | 1) Hydrophilic interactions (polar/electrically charged) hydrophilic outside 2) Hydrophobic interactions (nonpolar) hydrophobic inside 3) Hydrogen Bonds (polar) 4) Ionic Bonds (electrically charged) 5) Disulfide Bridge (2 cysteine aa/crosslinking |
| What determines protein structure? | PRIMARY STRUCTURE determines ultimate structure, but chemical and physical conditions can affect structure too; alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel - disrupts 2nd,3rd,4th stages |
| Denaturation | loss of a protein's native structure; biologically inactive/nonfunctional; affects secondary, tertiary, and quaternary when applicable but not primary |
| FOLD determines STRUCTURE; STRUCTURE determines FUNCTION | |
| Nucleic Acids | DNA and RNA |
| Polynucleotides | made up of monomers called nucleotides |
| Nucleotide is made up of 3 parts | Nitrogenous base, 5-carbon sugar, and a phosphate group |
| Nitrogenous Bases | 2 families: Purine and Pyrimidines |
| Purines | Larger; 6-membered rung fused to a 5-member ring |
| Pyrimidines | Smaller; single 6-membered ring |
| 5-Carbon Sugar | Carbons are counted and denoted by a number with a prime symbol (3') |
| Nucleoside | Nitrogenous base + 5-carbon sugar; nitrogenous base is bound to the 1' C of the deoxyribose sugar of DNA |
| Phosphate Group | Each nucleoside is bound to a phosphate group; bound to the 5' carbon of the 5-carbon sugar |
| Phosphodiester Linkage/Bond | Bond between two nucleotides happens at the 3'C of one nucleotide and the phosphate group of the other nucleotide |
| DNA vs RNA | DNA has T while RNA has U; DNA has only a H at 2' while RNA has OH |
| DNA is the instruction for making protein | |
| DNA shape | Helical, double helix, antiparallel, nitrogenous bases on the inside with the phosphate group and 5-carbon sugar on outside |
| Chargaff's Rules | Equal number of A and T, and an equal number of G and C bases; one purine + one pyrimidine |
| 5' end and 3' end | 5' end on the phosphate group and 3' end on opposite side |
| G-C | 3 Hydrogen Bonds |
| A-T | 2 Hydrogen Bonds |
| DNA structural model | 2 polynucleotides running antiparallel with 2 hydrogen bonds between A-T and 3 hydrogen bonds between G-C |
| Carbs | CHO |
| Fats | CHO |
| Proteins | CHON |
| Nucleic Acid | CHONP |
| Llinkages | Carbs - Glycosidic Lipids - Ester Protein - Peptide Nucleic Acid - |