Notes in Lecture Proteins and Enzymes 1

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Published	08/28/2024	Native protein structure is dicated by its {{c1::amino acid sequence {primary structure}}
Published	08/28/2024	Proteins start folding at the minimum energy state of the {{c1::molten globule states}}
Published	08/28/2024	Tertiary structure is formed via interactions among {{c1::secondary structure elements}}
Published	08/28/2024	Quaternary structure is formed by interactions among {{c1::protein/tertiary structure subunits}}
Published	08/28/2024	Hydrophobic collapse describes how a protein folds itself, where orientation of {{c1::hydrophobic}} amino acids are towards the {{c2::interi…
Published	08/28/2024	Supersecondary structures, or {{c1::motifs}}, are particularly stable arrangements of secondary structure elements
Published	08/28/2024	{{c1::Domain structures}} are distinct units of {{c2::secondary}} and {{c2::tertiary}} structure within a protein
Published	08/28/2024	The 4 main ways to denature proteins are:{{c1::HeatExtreme pHOrganic solventsdetergents}}
Published	08/28/2024	There are three main types of protein arrangements, which are:{{c1::α-Helicesβ-sheetsCollagen triple helix}}
Published	08/28/2024	Fibrous proeins are usually {{c1::structural}} proteins, are water-{{c1::insoluble}}, comprise {{c1::connective}} tissues, tendons, bon…
Published	08/28/2024	α-Helix are {{c1::insoluble protective structures of varying hardness and flexibility}}
Published	08/28/2024	β-conformation sheets are {{c1::soft, flexible filaments}}
Published	08/28/2024	Collagen triple helix are {{c1::high tensile}} strength without {{c1::stretch}}
Published	08/28/2024	a-Keratin provide {{c1::structural support}} for epithelial cells as intermediate filaments and have a {{c1::coiled-coil structure}} similia…
Published	08/28/2024	The {{c1::Leucine}} zipper motif is a type of a-Keratin.{{c1::Leu}} line up with each other and polar charges in the middle stabilize to create the st…
Published	08/28/2024	In a-Keratin, dimers become {{c1::protofilaments}} which then become {{c2::microfibril}}
Published	08/28/2024	Collagen is found in 25% of mammals and is a major component in {{c1::connective tissues}}. It is the most abundant protein found in mammals.&nbs…
Published	08/28/2024	The basic structure of {{c1::collagen}} is a {{c2::right-handed triple helix}} formed by {{c3::three left handed helical polypeptides}}
Published	08/28/2024	The amino acid sequence of collagen has abundant amounts of amino acid {{c1::Gly}} (at every third residue), and also has {{c1::Pro, Ser, Ala.}}{{c1::…
Published	08/28/2024	{{c1::Hyp, or hydroxyproline}} forms additional {{c2::hydrogen bonds}} that stabilize collagen
Published	08/28/2024	{{c1::Vit C}} is required to maintain activity of {{c2::prolyl hydroxylase}}
Published	08/28/2024	{{c1::Collagen fibrils}} are {{c2::not completely continous}} and resemble long ropes.
Published	08/28/2024	There are a total of {{c1::28 types}} of collagen that all vary in number of triple helix segments. Each contain various types of modificati…
Published	08/28/2024	{{c1::Type I-III}} collagens are {{c2::fibrous (connective tissue}}{{c2::Type IV}} collagens are {{c2::networks (basal lamina)}}
Published	08/28/2024	{{c1::Osteogenesis imperfecta}} is a {{c2::type I collagen defect}} that causes {{c3::brittle bones.}}{{c1::Ehlers-Danlos syndrome}} is a {{c2::type I…
Published	08/28/2024	Globular protein structures are influenced by their {{c1::environment}}
Published	08/28/2024	{{c1::Intrinsically unstructured proteins}} change structures upon {{c2::interaction with other proteins}}
Published	08/28/2024	{{c1::Metamorphic}} proteins exist in equilibrium between {{c2::functinoally distinct states}}
Published	08/28/2024	Once a {{c1::α-helix}} transforms into a {{c2::β-sheet}}, it enters a more stable configuration and will not revert back
Published	08/28/2024	{{c1::Amyloidoses}} are disease that result from formation of {{c2::protein aggregates}}, which are called {{c3::amyloid fibrils or plaques}…
Published	08/28/2024	Proteins can dynamically swap between {{c1::native}}, {{c1::molten globule}}, and {{c1::denatured}} forms. They can also {{c2::sel…
Published	08/28/2024	{{c2::Alzheimer disease}} is a result of {{c1::extracellular accumulation of amyloid-b(Ab) protein}}
Published	08/28/2024	{{c1::Amyloid-b(Ab) protein}} is associated with Alz's disease and results from {{c2::Phe amino acids pi-bonding}} to each other, transforming fr…
Published	08/28/2024	{{c1::CJD or Creutzfeld-Jakob disease}} is a heritable encephalopathy and results from aggregation of {{c2::pathological prior proteins (PrP -> PrP…
Published	08/28/2024	{{c1::Myoglobins and hemoglobins}} are related proteins that bind {{c2::oxygen}} using a {{c2::heme prosthetic group}}
Published	08/28/2024	Most metals have {{c1::6 coordination sites}}, which means there is only 1 empty spot for O2 to bind.In the case of oxygen binding to hemoglobin,…
Published	08/28/2024	Myoglobin is {{c1::monomeric}}, meaning it can only {{c2::bind 1 oxygen.}}
Published	08/28/2024	{{c1::Hemoglobin}} is {{c2::tetrameric}} meaning it can bind up to 4 O2 with two {{c2::α-chains 141 aa}} and two {{c2::β-chains 146aa}}
Published	08/28/2024	{{c1::Cooperative binding}} is when binding of one substrate causes a {{c2::conformational change}} that {{c3::allows much easier successive binding}}
Published	08/28/2024	{{c1::Deoxy}}hemoglobin is indicative of {{c2::T-state hemoglobin}} and overall {{c2::lower}} O2 affinity{{c1::Oxy}}hemoglobin is indicative…
Published	08/28/2024	Even the smallest changes caused by substrate binding in Hb are reflected, thus allowing for {{c1::cooperativity}}
Published	08/28/2024	{{c1::Allosteric effectors}} are substrates that bind to enzymes, changing efficacy and conformation
Published	08/28/2024	{{c1::2,3-BPG}} is an allosteric effector that stabilizes the {{c2::T-state}}, which overall {{c3::reduces oxygen affinity}} so that it can be un…
Published	08/28/2024	{{c1::Hemoglobinopathies}} encompass all genetic diseases of hemoglobin such as: {{c2::Thalassemia syndromesStructural hemoglobin variants (HbA, …
Published	08/28/2024	Deoxy HbS is termed {{c1::sickle cell anemia}} and results from deformation of fibers as a result of {{c2::Glu6 to Val6}} mutation.RBCs with thes…
Published	08/28/2024	Buffer equation:{{c1::CO2+H2O = H2CO3 = H+ + HCO3-}}
Published	08/28/2024	The Bohr effect describes the {{c1::change in oxygen binding affinity of hemoglobin}}, where {{c2::increased}} CO2 causes a {{c2::decrease}} in pH and…
Published	08/28/2024	{{c1::His146 protonation}} and {{c2::amino-termini carboxylation}} both stabilize the T-state
Published	08/28/2024	{{c1::Tertiary}} structure involves interactions between the R groups of amino acids.
Published	08/28/2024	Denaturing a protein usually leaves the {{c1::primary}} structure intact.
Published	08/28/2024	{{c1::Hydroxyproline}} allows for hydrogen bonding to occur in a peptides secondary structure. This is important in {{c2::collagen}} fibers.
Published	08/28/2024	Vitamin {{c1::C}} is required to form hydroxyproline for collagen fibers.
Published	08/28/2024	{{c1::Type IV}} collagen form networks instead of being fibrous (unidirectional).
Published	08/28/2024	At high altituted, our bodies produce more {{c2::2,3 BPG}} in order to shift the oxygen dissociation curve to the {{c1::right}}.
Published	08/28/2024	Suicide inhibitors are {{c1::acted upon}} by the enzyme.
Published	08/28/2024	Sometimes pH in our muscles is kept {{c1::lower}} in order for RBCs to release oxygen easier.
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