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Unit 2 Bio101
Biomolecule, acid base, carbon
| Term | Definition |
|---|---|
| Monomers | small building block that make up polymers Held together by covalent bonds |
| Dehydration reaction | Build up or make polymers (synthesize) Monomers form covalent bonds to synthesize a polymer, producing water. Often require energy input in form of ATP |
| Hydrolysis reaction | Used to break down polymers Polymers are broken down by adding a water molecule to the polymer. Releases energy, which may be captured as ATP |
| Sugar/Carbohydrate | "ose" ending |
| Glycosidic Linkage | Covalent bond that connects monosaccharides to each other |
| Functions of polysaccharides | Storage material for energy and structural support |
| Glycogen | Polysaccharide of long branching chains of glucose |
| Glucose | Most common monosaccharides, preferred substrate for energy production in many cells |
| Glycolysis | Breakdown of glucose into ATP -Breaking down covalent bonds between carbon atoms in glucose -Releases energy that was stored in bond, and transferring that energy into ATP |
| Storage Polysaccharides | Since glucose is a preferred source of energy, many cells store glucose in HUGE polymers made from chains of glucose Glycogen in animals Starch in plants |
| Cellulose | -Glucose polymer, provides struct in plant cells walls -Beta glycosidic linkages for chains -Chains can’t be broken by enzymes that break alpha linkages like in starch -“Insoluble fiber” in humans but other animals have bacteria can process linkages |
| Chitin | Forms cell walls Structural polysaccharide |
| Structural Polysaccharide | Cellulose and Chitin |
| Glucose polymer | a complex carbohydrate made of many glucose (simple sugar) molecules linked together by glycosidic linkages alpha-1,4 Iinkage in starch beta- 1,4 in cellulose |
| Lipid | Organic molecules based on hydrocarbons Not polymers because they don't get big, though some are made out of fatty acids |
| 3 important lipids | Fats - triglycerides Phospholipids Steroids |
| Fatty acid | comprised hydrocarbon chain with carboxyl group Amphipathic- head is hydrophilic, chain is hydrophobic Often floats on water, with head pointed down Can be used to make ATP |
| Fats | made of fatty acids triglycerides: molecules made when 3 fatty acid chains are linked together by a glycerol head Not water soluble Abundant in foods we eat, can be stored for future energy |
| Saturated fats | no double bond of carbon linear |
| Unsaturated fats | double bond of carbons not linear |
| Adipocytes | Dietary sources of fats can be stored in specialized cells called |
| Phospholipid structure and function | contains two fatty acid tails, attached by a head that includes glycerol and phosphate (hydrophilic) Tails are hydrophobic Amphipathic natures makes them assemble into bilateral in water (head attracted to water) Basis for plasma membranes |
| Protein structure and function | -Structural roles (form a lot of the structure of cells) -Energy Sources -Cell functions such as signaling, internal transport, contraction, transport of material across the cell membrane -Enzymes -Bodily defense |
| Protein structure is important for protein function | Proteins vary greatly in their structure These differences are always related to protein function |
| Protein Structure | Long chains of amino acids, connected by covalent bonds called peptide bonds Polypeptide chain Beginning of Chain is called N-terminus: Amino group End called C-terminus: Carboxyl group |
| N-terminus | Beginning of a protein chain where amino group is present (NH2) |
| C-terminus | End of a protein chain where carboxyl group is present (COOH) |
| Amino acids | Monomers that make up proteins (20 different types commonly found in animal proteins) The random order and length can generate infinite number of proteins |
| Primary structure | Sequence of amino acid chains makes up the protein's _____ |
| R groups | Different groups that vary on the amino acid; give amino acid their distinctive chem & physical properties Side chain Typically contain functional groups |
| Structure of an Amino Acid | Amino group, carboxyl group, and side chain (R group) Amino and carboxyl form peptide bonds (backbone of polypeptide chain) R group extends off to side of chain |
| R groups | Give amino acid their properties Determine how amino acid interacts with water, each other, and other molecules in cell In turn, these interactions affect the structure and properties of proteins |
| Amino acid interactions with each other within a single protein (which may change 3d shape of protein) | Depending on R group, neighboring amino acids may form -H-bonds (polar amino acids) -Ionic bonds (acidic and basic AA) -Di-sulfide bonds (Between R group with sulfur atoms) -Hydrophobic interactions and van der Waals interactions (nonpolar AA) |
| Secondary structure of protein | amino acid interactions 3d SHAPE r group between amino acids are interacting Alpha helices or Beta sheets |
| Alpha helices | Based on hydrogen bonds forming between polar amino acid side groups |
| Beta sheets | Based on a different pattern of hydrogen bonding between polar amino acid side groups |
| Tertiary structure of proteins | Internal interactions in proteins amino acids generate its 3d shape This structure is directly related to its function |
| Quaternary structure of proteins | Multiple subunits When multiple polypeptide chains aggregate (combine) to form a functional structure |
| DNA | stores genetic info for the cell Double stranded |
| RNA | helps translate the information stored in DNA to make the proteins needed for cell function Single stranded |
| Nucleotide structure | Nitrogenous base (one or two rings), sugar (ribose in RNA, deoxyribose in DNA), and a phosphate group |
| Nitrogenous base | Pyrimidines or Purines |
| Pyrimidines | single ring Cytosine, thymine (DNA only), and Uracil (RNA only) |
| Purines | Double ring Adenine and guanine |
| Phosphate group | Nucleotides can polymers when this group bonds with the sugar group of another nucleotide Yields a phosphate-sugar backbone and nitrogenous bases extending to the side of the chain |
| 5' end of a nucleotide | Has a free phosphate group |
| 3' end of a nucleotide | Has a free sugar |
| DNA structure | antiparallel chains with complementary sequence A form 2 hydrogen bonds with T C form 3 h-bonds with G 5' end paired with 3' end of other strand |
| mRNA | type of RNA that is transcribed from a DNA Contains the instructions for building proteins, specific "codes" within the mRNA polypeptide chain These proteins then go on to do much of the work of the cell How DNA encodes instructions for life (by encod |
| Central dogma | DNA holds the genetic code, which is transcribed into messenger RNA (mRNA) in the nucleus. This mRNA then moves to the cytoplasm and is translated by ribosomes into proteins, which are now functional molecules that carry out various tasks in the cell. |
| Watson and Crick | Credited for identifying the structure of DNA, won a Nobel piece prize |
| DNA functions | template to generate DNA Store genetic info, replicate itself by passing info to new cells, and allow gene expression to create proteins & other functional molecules |
| RNA functions | messenger, translate between DNA and amino acid sequence (central process of protein synthesis) Also serves in gene regulation, controlling when and where genes are expressed |
| Acids and bases affect living organisms | Occasionally a hydrogen atom will shift from one water molecule to another An electron (-) is left behind forming the hydroxide ion (OH-) and the hydrogen ion (+) is transferred (H3O+) |
| Acids | add (donate) H+ to the solution Will increase [H+], lowering pH 0-6 on pH scale |
| Bases | remove (accept) H+ from the solution Will decrease [H+], increasing pH 8-14 on pH scale |
| How do acids and bases affect other molecules? | Generate charged ions (H+) or (OH-), which can disrupt bonds These types of bonds are important for forming the 3d structures of molecules (proteins & nucleic acids) Denaturation of a protein Cells in stomach secret HCl, a strong acid for digestion |
| Denaturation of a protein | When ionic & h-bonds that hold a protein 3-D shape, are broken by acids or heat |
| Buffers | stabilize pH in solution Minimize changes in H+ of OH- by accepting or donating H+ |
| Buffer example | Carbonic acid (H2CO3) will be added to water, creating H30+ and HCO3-(bicarbonate acid) This happens in the stomach but also can happen in the bloodstream |
| Isomers | molecules with the same molecular formula but different structure/arrangement |
| Cis-isomer | The two XS are on the same side |
| Trans-isomer | The two XS are on the opposite side |
| Enantiomers | mirror image (L isomer and D isomer) |
| Functional groups | Chemical structures frequently found in organic molecules |
| Hydroxyl groups | -OH- polar Compound name - Alcohol Makes molecule experience H-bonding (duh) |
| Carboxyl groups | -COOH- Can act as acid and carry negative charge Compound name: Carboxylic or organic acid |
| Amino groups | -NH2- can act as base, carry + charge Amine |
| Methyl groups | -CH3- Gene expression Hormone function |
| Phosphate groups | -OPO3 2- Organic phosphate can act as acid |
| Basic solution examples | Seawater, inside of small intestine Milk of magnesia Household ammonia Household bleach Oven cleaner |
| Acidic solution examples | Battery acid Gastric juice (stomach) Lemon juice Vinegar, wine, cola, formic acid Tomato Juice, beer Black coffee, rainwater Urine, Saliva |
| Nonpolar molecules | BrINClOF - diatomic elements bonding with itselfs Tetrahedrals with same element Don't dissolve in water, hydrophobic |
| how we get nitrogen | air and soil, courtesy of bacteria and fungi that "fix" it and share it with plants |
| 7 strong acids | fully dissociate in water H2SO4 , HCl, HBr, HI , HNO3 , HClO4 , HClO3 |
| Difference between beta sheets and alpha helices | Alpha helices r coiled spiral-like structs stabilized by h-bonds b/w backbone atoms w/in single polypeptide chain Beta sheets r extended sheet-like structs formed by multiple beta strands linked by hbonds b/w backbones of adjacent strands |
Created by:
phillipchristopherr
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