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Bio 1 Week 2 Notes

by: clb13m

Bio 1 Week 2 Notes BSC2010

GPA 3.8

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Goes over the cellular membrane and structure
Biological Science 1
Dr. Steven Marks
Class Notes
Biology 1
25 ?




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This 4 page Class Notes was uploaded by clb13m on Monday January 11, 2016. The Class Notes belongs to BSC2010 at Florida State University taught by Dr. Steven Marks in Fall 2015. Since its upload, it has received 39 views. For similar materials see Biological Science 1 in Biological Sciences at Florida State University.

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Date Created: 01/11/16
 Know the structure and general chemical activities of the major reactive groups on organic molecules, OH  (hydroxyl, basic, hydrogen bonding), CO & CHO (carbonyl, hydrogen bonding), NH2 (amine, basic,  hydrogen bonding), COOH (carboxyl, acidic) P04 (phosphate, charged and high energy bonds), SH  (sulfhydryl, reactive, important in protein structure), CH3 (methyl, non reactive and nonpolar) o Hydroxyl (–OH) – alcohol; polar o Carbonyl (C=O)/(H­C=O) – ketone if the carbonyl group is within a carbon skeleton/aldehyde if  the carbonyl group is at the end of the carbon skeleton o Carboxyl (O=C­OH) – has acidic properties because the covalent bond between the oxygen and  hydrogen is so polar o Amino (H­N­H) – amines; in amino acids; acts as a base o Sulfhydryl (­SH) – thiols; two sulfhydryl groups can react, forming a covalent bond. This “cross­ linking” helps stabilize protein structures o Phosphate (PO4) – contributes negative charge to the molecule of which it is a part (2­ when at the end of a molecule, 1­ when located internally in a chain of phosphates); activity of proteins is  often controlled by the addition or removal of phosphate groups; bonds are high energy bonds and  are often used as energy currency in cells (ATP) o Methyl (CH3) – addition of a methyl group to DNA, or to molecules bound to DNA, affects  expression of genes  Be able to distinguish carbohydrates (sugars), lipids, and amino acids from their structural formulas. Know  what a monosaccharide, disaccharide, and polysaccharide are, that glucose is a 6 carbon monosaccharide. o Carbohydrates – sugars and the polymers of sugars source of energy and carbon  Monosaccharide – single sugar molecular formulas (simplest carb)  Disaccharide – double sugars (two monosaccharides)  Polysaccharide – polymers composed of many sugar building blocks o Lipids o Amino Acids  Know that glucose forms two important polysaccharides, starch (glycogen) and cellulose. Starch is used for energy storage and that cellulose is used in plants to build cell walls (has a  structural role). o Starch – plants store stockpiles of glucose in the form of starch in chloroplasts  Two forms: Amylose (linear chain of 1­4 glycosidic linkages) and amylopectin  (branched, has additional 1­6 linkages) o Cellulose – major structural component of the tough wall of plant cells; cellulose is a polymer of  glucose, but the glycosidic linkages differ from starch. The difference is based on two ring forms  for glucose: alpha (starch) and beta (cellulose)  Know the general structures of the three types of lipids (Fats, Phospholipids, and Steroids) and be able to  state what their main biological functions are.  o Fats – energy storage  Fatty acids may be saturated (all carbons have two attached H) or unsaturated (some  carbon­carbon double bonds)  Most animals are saturated. These fats stack together to form solids (butter). Can clog  arteries and cause cardiovascular disease  Unsaturated fats are prevalent in plants and fish. The inflexibility of double bond  prevents them from stacking. Thus they are liquid at room temperature o Phospholipids – building membranes  Two fatty acids and a phosphate group are attached to glycerol; the fatty acid tails are  hydrophobic, but the phosphate group forms a hydrophilic head o Steriods – are signaling molecules (hormones)  They’re lipids characterized by a carbon skeleton consisting of four fused rings  Cholesterol, implicated in cardiovascular disease; it’s a component in animal cell  membranes and is the precursor to several steroid hormones  Know that proteins are polymers of amino acids held together by peptide bonds, that each kind of protein  has a unique amino acid composition (different order in which the amino acids are strung together), that  cells contain thousands of different kinds of proteins and that each protein has a specific cellular function. o The different R groups have different sizes, shapes, and chemical properties o Major groups are nonpolar, polar, and charged o Its this variety in the R groups that give proteins their diverse functions  Be able to draw the general structure of an amino acid, know that there are 20 different amino acids used to make proteins, and know the four different categories of amino acids based on the chemical character of  their R groups (side groups) ­­ nonpolar, polar but uncharged, charged (acidic or basic). o Four different categories: Nonpolar, polar, polar Acidic (charged), polar basic (charged) o Amino Acids are joined by peptide bonds  A linear chain of amino acids is a polypeptide, which have amino and carboxyl ends  Functional proteins consist of one or more polypeptides ­  Know what the 4 levels of protein structure are  (primary through quaternary). Know that the  tertiary structure of a protein is stabilized by interactions between amino acid R groups within a  polypeptide, that these interactions are hydrogen bonding between polar but uncharged R groups, ionic  bonds between charged amino acids, covalent disulfide bonds pairs of cysteins, and hydrophobic  interactions (Van der Waals interactions) between amino acids with nonpolar R groups. o Primary – sequence of amino acids in the chain o Secondary – regular, repeating hydrogen bondig between the N and O components of peptide  bonds  In A helix, H bonding causes coiling  In B pleated sheets, H bonding causes kinks o Tertiary – creates overall 3­D shape, resulting from interactions between R groups o Quaternary – overall structure when two or more polypeptides interact to form the active protein;  interaction between polypeptides are the same as those involved in tertiary interactions  Understand what "denaturation" and renaturation of a protein means; that heat or high or low pH can cause  proteins to denature, and that denatured proteins are inactive (lose their function). o Denaturation – loss of 3D structure; does not function  Caused by high heat, high or low pH, anything that disrupts interactions that hold  structure together o Renaturation – functional proteins, although not all proteins an renature once they are denature  Were denatured, then the 3D structure was rediscovered  Know the general structure and function are of the following cellular structures and organelles: plasma  membrane, nucleus, ribosomes, ER (rough and smooth), Golgi, lysosomes, mitochondria, and chloroplasts.  Be able to identify each of these organelles in photographs or drawings of cells. o Plasma membrane ­ is a biological membrane that separates the interior of all cells from the  outside environment. The cell membrane is selectively permeable to ions and organic molecules  and controls the movement of substances in and out of cells. o Nucleus ­double membrane; prorated by nuclear pores; ribosomes & mRNA made in nucleolus o Ribosomes ­ synthesize proteins (free or bound); get transported to other parts of the cell by  transport vesicles o Rough ER ­ ribosomes in RER make membrane proteins and proteins to be secreted; these  proteins are transported to other parts of cell by transport vesicles; membrane factory for cell o Smooth ER ­ synthesis of lipids; storage of calcium o Golgi ­ sorts and moves membranes and proteins made in ER; vesicle merges and dumps sack  from the ER to the golgi. The stuff in the sack gets sorted/relocated to its correct place o Lysosomes ­ contain enzymes that help digest food or defective macromolecules or organelles to  recycle their components  Phagocytosis – lysosome digests food in the food vacuole that was taken into the cell  Autophagy ­ picks up organelles thats dying o Mitchondria ­ membrane bound organelle; have own DNA/ribosomes for making its own proteins; transforms energy from one form to another; used for cellular respiration o Chloroplasts ­ membrane bound organelle; have own DNA/ribosomes for making its own  proteins; transforms energy from one form to another; used for photosynthesis  Understand that the pathway for the flow of materials to the cell surface is from ER to the Golgi, to Golgi  vesicles, to the plasma membrane o Vesicle goes from rough ER to cis Golgi, gets transported to transexual golgi, then is determined  whether it gets transported to the lysosome, plasma membrane, or wherever the protein inside the  vesicle tells it to go (mRNA)


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