MCB 150 Study Guide Exam 1 PDF

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Study guide/learning objectives for Exam 1 in MCB150...

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Learning objectives: ● Compare and contrast the three domains of life, explaining how sequence data can determine evolutionary relationships  ● Describe the features of a plasma membrane, including why cells remain in a relatively narrow size range  ● Identify the features of a bacterial cell and interpret their functions  ● Identify the major organelles in an animal cell and list their functions  ● Compare and contrast condensation and hydrolysis reactions, and their relationship to macromolecules and monomers  ● Identify the general properties of carbohydrates and the specific properties of biologically-relevant monosaccharides  ● Provide examples of the functions of carbohydrates in cells  ● Describe the formation of a glycosidic linkage and classify it in the most specific terminology available ●  ● Describe the type of monomer, the type of linkage, the branching (if any), and the major functions of the following polysaccharides: starch, glycogen, and cellulose

 ● Describe the general structure and classification of an amino acid, and the consequence of being in a given class  ● Explain the directionality and general process of peptide bond formation  ● List the levels of protein organization and identify the stabilizing forces at each level  ● Describe the process of protein denaturation and renaturation, including the use of chaperones when necessary  ● Explain reactions in terms of energy transfer and change in free energy  ● Explain the energy of activation of a reaction and how it is decreased in the presence of enzyme  ● Describe the conditions that affect or inhibit enzyme activity

 ● Identify how the structure of a nucleotide leads to the properties of a nucleic acid  ● Explain the formation of a phosphodiester linkage and how cells use nucleic acids  ● Describe the cellular functions of lipids and why they are not as easily categorized as the other macromolecules in a cell  ● Describe the structure and nomenclature of fatty acids and their condensation into triglycerides and phospholipids  ● Define and explain the structure and properties of phospholipids and biological membranes  ● Describe the structures and roles of membrane glycolipids and steroids  ● Compare and contrast the 4 major types of membrane proteins

 ● Analyze the properties that affect membrane fluidity, and the movements of the lipids in that membrane  ● Identify the components and functions of an animal cell plasma membrane Peripheral membrane proteins: non-covalent (usually there for attachment to something)  Integral membrane proteins: disrupts integrity of the membrane to remove the protein Transmembrane proteins: cross both leaflets atleast once Membrane association proteins: go in, but go back out (dont go i all the way) (usually there for attachment to something) lipid-linked: covalently attached to a membrane lipid Breaking or making covalent bonds: enzymes Sugars have no known catalytic activity (carbs aren't enzymes) Who would they feed? Wouldn't be C Glycoprotein v glycolipid: Dehydration synthesis= condensation reactions

Peroxisome: detoxify things  + Delta g, anabolic, biosynthetic, endergonic Building something  Phospholipid can spin around/flex (1000x/sec) Lateral shift: not turning over, not leaving leaflet Flipping of phospholipid: transverse diffusion Asymmetry: Energetically unfavorable but needs to happen quickly==== enzyme  Protein synthesis : n to c terminus Amino group will interact w carboxyl group that was already there  C bonded to n and double bonded to o, n bonded t c and H, thats a link 

Chaperones are NOT enzymes Chaperones An entirely dif set of proteins; proteins assisting in the proper folding of an unfolded protein  Allosteric regulation: can bind reg molecule to site on enzyme (not on active site) (can make you better OR worse at job)  Non-comp inhibition: synonymous  More unsaturated, more kinks, more fluidity Cholesterol stabilizes membrane thats abt to melt away or “bust up interactions” b/t 5’-3’ Phosphate attached to 5’ of incoming is going to chemically attach to the hydroxyl of the 3’ already there Amphipathic: ( of a molecule, especially a protein) having both hydrophilic and hydrophobic parts.

 ATP= nucleoside triphosphate

Relative electronegs = non-polar Nucleoside: sugar + nitrogenous base Fine tune kinks, shorten/lengthen tails (steroid job) Cholesterol is a steroid (4 ring w iso tail) and mods to cholesterol make dif hormones permeability increases when fluidity increases As stability increases, permeability decreases PRIONS: protein in our CNS (normal when folded correctly)...