Cell Biology Chapter 2
Cell Biology Chapter 2 BIOL 225
Popular in Cell Biology
verified elite notetaker
Popular in Biology
verified elite notetaker
This 5 page Class Notes was uploaded by MelLem on Saturday January 30, 2016. The Class Notes belongs to BIOL 225 at Simmons College taught by Dr. Lopilato in Fall 2016. Since its upload, it has received 41 views. For similar materials see Cell Biology in Biology at Simmons College.
Reviews for Cell Biology Chapter 2
Report this Material
What is Karma?
Karma is the currency of StudySoup.
You can buy or earn more Karma at anytime and redeem it for class notes, study guides, flashcards, and more!
Date Created: 01/30/16
Cell Biology BIOL 225 Chapter 2 – The Chemical Basis of Life Important Functional Groups to Consider Types of Bonds • Covalent Bonds – Sharing of electrons, strong bonds, 80-‐100 kcal/mol to break bonds. • Non-‐covalent Bonds – Attractive forces between molecules, weaker bonds 1-‐5 kcal/mol to break bonds. Non Covalent Bonds • Ionic Bonds – Between charged molecules • Hydrogen Bonds – between polar molecules • Hydrophobic interactions & Van Der Waals Forces – between nonpolar molecules. Macromolecules • Macromolecules can be divided into four separate and major categories, they are: o Nucleic Acids o Proteins o Polysaccharides o And certain Lipids • Monomers are the basic unit, multiples of these units create a polymer. • Ex: 2 monosaccharides = disaccharide (sucrose) Properties of Amino Acids • R groups – o Charged / Uncharged o Polar / nonpolar o Unique propert Types Of Amino Acids in Classifications (Memorize, be able to recognize R Groups) • A peptide bond is a covalent bond Protein Structure Importance • Misfolded proteins can be deadly and cause disease. • The order of amino acids (primary Structure of proteins) determines the Tertiary and Quaternary Structures. Protein Structure • Primary Structure – order of amino acids determines this • Secondary Structure – Hydrogen bonds • Tertiary Structure – Three Dimensional shape of a single polypeptide • Quaternary Structure – Two or more polypeptide subunits o These subunits are identical making them homodimer. o Non identical subunits however are called hertodimer. o They are held together by a covalent and/or non covalent bonds. Denatuartion and Renaturation • Denaturation – the unfolding of proteins, proteins that have this happen to them lose their function. Denaturation can happen because of heat, detergents, organic solvents and other compounds. o When the conditions reverse, proteins renature – meaning they fold back into there tertiary and quaternary structures (primary structure is the order of amino acids) Carbohydrates • Monosaccharides o # of carbon atoms o Aldo or Keto sugar o Ring formation o Modifications • Glycosidic Bond • Disaccharides • Oligosaccharides • Polysaccharides • If a carbonyl group C = O is located on an internal position the sugar is ketose • If the carbonyl group is on top end of the molecule, it is known as an aldose. Polysaccharides • Bonds – αVs. β-‐ • Polysaccharides o Storage ▯ Starch – amylose & Amylopectin ▯ Glycogen o Structure Nucleic Acids • Monomer = nucleotide • Polymer = DNA & RNA • Phosphodiester bonds – covalent • RNA – single stranded and secondary structure • DNA – double stranded Characters of Lipids • Triglycerides = glycol Backbone • Sphingosines + cerebroside backbone o Non-‐polar, hydrophobic tails o Charged group heads • Lipids and proteins have sugars attached to them in their membrane • Cholesterol = steroid • Kinked chains come from double bonds and the lack of hydrogen
Are you sure you want to buy this material for
You're already Subscribed!
Looks like you've already subscribed to StudySoup, you won't need to purchase another subscription to get this material. To access this material simply click 'View Full Document'