5. Notes on Nylon, Amino acids, Keratin, Collagen, Gelatin
5. Notes on Nylon, Amino acids, Keratin, Collagen, Gelatin LSM1401
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This 0 page Class Notes was uploaded by HAN ZIXUAN on Thursday November 5, 2015. The Class Notes belongs to LSM1401 at National University of Singapore taught by Jayaraman Sivaraman in Fall 2015. Since its upload, it has received 41 views. For similar materials see Fundamental of biochemistry in Biology at National University of Singapore.
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Date Created: 11/05/15
Brief Notes L5 Nylon 1 Monomers form dimers trimers tetramers l 2 Multimers combine to form small fragments l 3 Small fragments combine to form polymers Nylon 66 6C diamine hexamethylene diamine 6C diacid adipic acid 7 Nylon is an arti cial silk invented in 1935 as a rst synthetic ber by Wallace MONOMER dlammed39aad Carothers Nylon can be obtained by reacting an acid and a base The reaction covalentbond amidebond between a dicarboxylic acid and a diamine will result in the formation of a polyamide 6 6 Nylon by forming the amide bond A polymer may contain quotnquot POLYMERpolyamide nylon number of polyamides The polymers interact selfassembly through crosslink 055W Hhonds hydrogenbond and form the ber Crystallinity ordered structure drastically improves the mechanical property such as stiffness melting point and yield to FlBER stress of the polymer Crystallinity is the degree of structural order in a solid Crystallized vs Amorphous Crystallinityh Melting point DensityT Stiffness Yield stressT Amino acids Amino acids aa have amino and carboxyl groups There are 20 common amino acids in nature that form into proteins These amino acids can be grouped into different categories such as nonpolar no charge aa aromatic aa positively charged basic aa and negatively charged acidic aa Amino acids join together to form amide bond peptide bond ie the carboxyl group of one aa reacts with the amino group of the other aa releasing a water molecule H20 a condensation reaction 1 structure peptide Structures associated with peptides and proteins The primary structure is the linear order of aa sequence in the peptide or protein A peptide is a chain of amino acids The direction of the peptide is from Nterminal amino gp of rst aa to Cterminal carboxyl gp of last aa The peptide bond is xed all the atoms associated with the peptide bond are in one plane direction 39 31 stand 2 structure Bstrand amp Bsheets A Bstrand is a stretch of 3 or more linear aa it should be part of a Bsheet Two or more Bstrands form one B sheet The hydrogen bond crosslink between the backbone atoms of the adjacent Bstrands will maintain the 3 sheet assembly Parallel Bsheet all B strands run in the same direction either NDC or Cle Antiparallel Bsheet combination of both directions Example of Bsheet fiber is the spider silk parallel 2 structure uhelix helical cxhelix resembles a spring and is a helical like structure The W systematic hydrogen bonding contacts between the mainchain 7 atoms maintain the helical arrangement In several proteins the cx m Coiledmnhelixbu e helices form a c0Iledc0l structure like a thread In the rope The mW39Wm nv mmm 6 coiledcoil arrangement is mostly due to the systematic presence of w mmh l 1 some speci c aa in the helices involved in coiledcoil Keratin and collagen are the best examples of coiledcoil helical bundle structures Keratin is a brous protein that is the main component of hair Four keratin molecules tetramer coiledcoil bundle form proto laments then l proto brils then l keratin laments Or simply the keratin molecules copolymerize to form laments Collagen 1 collagen sequence D 2 single collagen polypeptide chain coi together to form D 3 triple helices bundle assembles to form D 4 collagen brils then 5 coagen bers The repeating sequence GIyProX X means any aa forms the systematic interaction and forms the triple helical bundle arrangement in collagen The collagen triple helices are stabilized by 1 Steric repulsive forces between the Proline within the monomer that will keep them away and 2 the inter chain hydrogen bond among the monomers chains that will form the helical bundle arrangement and stabilize the collagen triple helix Gelatin is an ancient product of collagen biotechnology Heating dissociates collagen triple helices into monomers and cooling systematically reassociates the monomers and forms gelatin Collagen has several applications in medicine biotechnology and in the cosmetics Hangman aliphatic gmups coo E l ELIE F I ll Hattie QH HI Elly i3 Glycine EDD HEN l H E 3H3 Leucine LEUL L cm Na a Alanine Fill a Ha tha i Methinine ME EM CUE g l H UH CH3 Valium Val iii i HEM c ll Ianleucine E Montana 11 gr 39 p EDD Pile F Fhenylal airline Hgg r if H EDDquot Tyr i Tarmaatine W39yp39tppirla n Trp Pillar uncharged H EDIE HEN 11 Il SHEDH Earl my Bar 8 SW gin HEN HIFH39E Ham WEE Praisier Pro Fquot NP P PWN lif Elgar Aif Il REEF DH EH3 Tili liemiiim Thr T and ILILIi xiT II EH2 E f HEN n ailill agi IllIL39 Hall H can HQN H helpline Bill39s I can HER E H HEN 1 Gilli l m Gill Explain a simple polyamide formation What is a peptide Explain with example P aitiively chargeti grougpa EDD Lysine Lyra K i ELM 4 BUD EGG unlike H CHE Em 32 iiiJEIE pic r z mg Arginine lig R Hiatidine HlEZ H Negativ ly charged R groups odor rh ty a 00 Aspa rtate Asp El HJi C li ll Glutamate Gilli E Who invented the rst synthetic ber When What is polymerization Explain with an example What is an amino acid Explain with example What is crystallinity What are its in uences in the properties of polymer Write the full names and classi cation of the amino acids R D K F W N Q E and Y NP P PWN What is a peptide bond Draw and explain with an example Describe the Bsheet and Bstrand structures What is a parallel and an antiparallel Bsheet Given an example of a Bsheet ber What is an cxhelix How is the coiledcoil helices formed Give examples Describe the structure of a collagen triple helix How is it stabilized List any 3 applications of collagen List and brie y explain the key steps involved in gelatin formation How are the amino acid Glycine and Proine different from other amino acids Glycine do not have any side chain and because of that it is exible than other amino acids Proine the side chain fused with the main chain amino group NH and because of that it is very rigid The ring structure of Proine is different from that in His Phe Tyr Typ whose ring structure are side chain rings independent or separate rings not fused with the main chain atom These type of features are not observed in the other amino acids
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