Sinh học - Chapter 4: Protein 3 - Dimensional structure and function

Loops Loops usually contain hydrophillic residues. Found on surfaces of proteins Connect alpha-helices and beta-sheets Turns Loops with < 5 AA’s are called turns Beta-turns are common

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Chapter 4Protein 3-Dimensional Structure and FunctionTerminologyConformation – spatial arrangement of atoms in a proteinNative conformation – conformation of functional proteinProtein ClassificationSimple – composed only of amino acid residuesConjugated – contain prosthetic groups (metal ions, co-factors, lipids, carbohydrates) Example: Hemoglobin – HemeProtein ClassificationOne polypeptide chain - monomeric protein More than one - multimeric protein Homomultimer - one kind of chain Heteromultimer - two or more different chains(e.g. Hemoglobin is a heterotetramer. It has two alpha chains and two beta chains.)Protein ClassificationFibrous –polypeptides arranged in long strands or sheetswater insoluble (lots of hydrophobic AA’s)strong but flexibleStructural (keratin, collagen)Globular –polypeptide chains folded into spherical or globular formwater solublecontain several types of secondary structurediverse functions (enzymes, regulatory proteins)keratincollagencatalaseProtein FunctionCatalysis – enzymesStructural – keratinTransport – hemoglobinTrans-membrane transport – Na+/K+ ATPasesToxins – rattle snake venom, ricinContractile function – actin, myosinHormones – insulinStorage Proteins – seeds and eggs Defensive proteins – antibodies4 Levels of Protein StructureNon-covalent forces important in determining protein structurevan der Waals: 0.4 - 4 kJ/mol hydrogen bonds: 12-30 kJ/mol ionic bonds: 20 kJ/mol hydrophobic interactions: <40 kJ/mol1o Structure Determines 2o, 3o, 4o StructureSickle Cell Anemia – single amino acid change in hemoglobin related to diseaseOsteoarthritis – single amino acid change in collagen protein causes joint damageClasses of 2o StructureAlpha helixB-sheetLoops and turns2o Structure Related to Peptide BackboneDouble bond nature of peptide bond cause planar geometryFree rotation at N - aC and aC- carbonyl C bondsAngle about the C(alpha)-N bond is denoted phi (f)Angle about the C(alpha)-C bond is denoted psi (y)The entire path of the peptide backbone is known if all phi and psi angles are specifiedNot all f/y angles are possible Ramachandran PlotsDescribes acceptable f/y angles for individual AA’s in a polypeptide chain.Helps determine what types of 2o structure are presentAlpha-HelixFirst proposed by Linus Pauling and Robert Corey in 1951 Identified in keratin by Max Perutz A ubiquitous component of proteins Stabilized by H-bondsAlpha-HelixResidues per turn: 3.6 Rise per residue: 1.5 Angstroms Rise per turn (pitch): 3.6 x 1.5A = 5.4 Angstroms amino hydrogen H-bonds with carbonyl oxygen located 4 AA’s away forms 13 atom loopRight handedhelixAlpha-HelixAll H-bonds in the alpha-helix are oriented in the same direction giving the helix a dipole with the N-terminus being positive and the C-terminus being negative Alpha-HelixSide chain groups point outwards from the helixAA’s with bulky side chains less common in alpha-helixGlycine and proline destabilizes alpha-helixAmphipathic Alpha-Helices+One side of the helix (dark) has mostly hydrophobic AA’sTwo amphipathic helices can associate through hydrophobic interactionsBeta-Strands and Beta-SheetsAlso first postulated by Pauling and Corey, 1951 Strands may be parallel or antiparallel Rise per residue: 3.47 Angstroms for antiparallel strands3.25 Angstroms for parallel strandsEach strand of a beta sheet may be pictured as a helix with two residues per turnBeta-SheetsBeta-sheets formed from multiple side-by-side beta-strands.Can be in parallel or anti-parallel configurationAnti-parallel beta-sheets more stableBeta-SheetsSide chains point alternately above and below the plane of the beta-sheet2- to 15 beta-strands/beta-sheetEach strand made of ~ 6 amino acidsLoops and turnsLoopsLoops usually contain hydrophillic residues.Found on surfaces of proteinsConnect alpha-helices and beta-sheetsTurnsLoops with < 5 AA’s are called turnsBeta-turns are common Beta-turnsallows the peptide chain to reverse direction carbonyl C of one residue is H-bonded to the amide proton of a residue three residues away proline and glycine are prevalent in beta turns

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