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Ap Bio: Macromolec.

QuestionAnswer
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 -
Created by: johnmkim2005
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