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Structure and Function of AAs and Proteins
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thirteen-gee-lemon-oven-spring-sodium
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The commonly phosphorylated uncharged polar AAs are {{c2::serine, threonine, and tyrosine}} because they have {{c1::-OH}} groups.
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6 uncharged polar AAs: {{c1::serine, threonine, tyrosine, asparagine, glutamine, cysteineSimone tumbles through all games courageously.}}
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9 nonpolar AAs: {{c1::glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, prolineGolfers are valiant, leading i…
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2 acidic side chain AAs:{{c1::aspartic acid and glutamic acid}}
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3 basic AAs: {{c1::histidine, lysine, arginine}}
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2 AAs with sulfurs: {{c1::cysteine, methionine}}
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{{c2::Disulfide}} bonds occur between {{c3::2 cysteine AAs}} in an {{c4::oxidizing}} environment. This bond is catalyzed by {{c5::protein disulfide is…
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{{c1::Methionine}} is specified by the codon AUG (start codon) and is therefore the first AA incorporated into eukaryotic proteins.
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{{c1::Formyl-methionine}} initiates protein synthesis in prokaryotes like bacteria
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nucleic acids are always written {{c1::5' to 3'}}
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three mRNA stop codons: {{c1::UGA, UAA, UAG}}
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{{c1::sickle cell anemia}} is the most frequent genetic disease among African Americans. It is a {{c2::missense}} mutation ({{c3::glutamic acid -->…
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{{c1::Cystic fibrosis}} is the most frequent genetic diseases among Caucasians. This is a deletion mutation because {{c2::deltaPhenylalanine (AA) is d…
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{{c1::primary structure}}: linear sequence of amino acid structural units
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{{c1::secondary structure}}: local folded structure like an alpha helix (alpha helix, beta pleated sheets)
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{{c1::tertiary structure}}: 3-D arrangement of a protein molecule ex. disulfide bridge, hydrophobic bonds)
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{{c1::quaternary structure}}: four globin chains forming a tetramer like hemoglobin
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What is the physiology behind sickle cell anemia and its missense mutation?{{c1::Glutamic acid (hydrophilic) is substitued with valine (hydrophobic) c…
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list the DNA mutation from greatest severity of damage to least: {{c1::frameshift, nonsense, missense, silent}}
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trasnsition point mutations are from {{c1::purine to purine}}
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trasnversion point mutations are from {{c1::purine to pyrinidine}}
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single nucelotide mutations in protein coding regions can lead to (x4):{{c1::- silent mutation no change- similar AA - minimal effect- different class…
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frameshift mutations are for the deletion/addition of {{c1::one or two}} nucelotides that reult in misreading of all nucleotides downstream
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{{c1::Hydroxyurea}} helps patients with SCD because it {{c2::increases fetal hemoglobin synthesis}} which reduces the concentration of sickled red cel…
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Most enzymes are {{c1::proteins}}.
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RNA molecules with enzymatic activity are called {{c1::ribozymes}}
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{{c1::Enzymes}} are highly selective biological catalysts that accelerates a chemical rxn without being consumed
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Enzymes end with {{c1::----ase}}.
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{{c1::human cells}} can make both protein and ribozymes
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simple enzymatic rxn: {{c1::E+S <- -> ES -> EP -> E + P}}
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Every enzymatic rxn goes through a {{c1::transition}} state which requires energy to get to. Enzymes decrease the {{c2::free energy of activation}} re…
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A substrate in its transition state has reached its {{c1::best fit with the enzyme}}. Effective {{c2::inhibitors}} of enzymes mimic T* (ex. HIV protea…
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HIV protease is a {{c3::symmetrical dimer}} and normally cleaves the {{c1::Phenylalanine-Proline peptide bond}}. Protease inhibitors are a breakthroug…
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A long HIV viral precursor protein is cleaved by {{c1::virally-encoded protease}} resulting in functional/required proteins for viral assembly. {{c2::…
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For enzymes, a {{c1::low Km}} means high affinity to substrate because there doesn't need to be a lot of the enzyme to bind to the substrate.
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2 main goals for every living species:{{c1::survive and propagate species}}
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4 ways to activate survival mode:{{c1::- cleave precursor proteins- change conformation of proteins by physical binding- change conformation by covale…
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Cleavage by {{c1::proteolysis}} activates inactive proteins
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cleavage by proteolysis pathway for angiotensin:{{c1::}}
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cleavage by proteolysis pathway for the blood clotting pathway: x2{{c1::}}
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describe the proteolysis pathway for digestive enzymes: x2{{c1::}}
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{{c1::Adenylyl cyclase (AC)}} is regulated by {{c2::allosteric}} changes. AC converts {{c3::ATP to cAMP}} which acts as a second messenger. When {{c4:…
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Altering {{c1::cAMP}} levels can increase cardiac output in seconds.
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explain GIa subunit on heart and AC:{{c1::}}
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explain GSa subunit effect on heart and AC:{{c1::}}
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Our blood vessels and airways constrict or relax by {{c1::covalently modifying myosin light chain}} in {{c2::smooth muscle}} cells which surround bloo…
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the smooth muscle contraction pathway can either contract or relax based on the state of {{c3::phosphorylation of the myosin light chain}} (a part of …
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Phosphorylation refers to the {{c1::addition of a phosphate group}} to a molecule- phosphorylation of the myosin light chain by a kinase enzyme l…
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Smooth muscle contraction pathway: {{c1::epinephrine or acetylcholine activates the Gq protein coupled recptor (GPCR) pathway --> increase in calci…
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Smooth muscle relaxation pathway: {{c1::albuterol triggers an increase in cAMP levels; nitroglycerin/nitric oxide triggers an increase in cG…
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