University:
Boston University
Course:
GMS AN 708 | Clinical Anatomy
Academic year:

2022
Views:

206

Pages:

8
Author:

SpaceCadet101

structural levels of proteins N Ala ser Cys Gly sequence of a as linked by peptide bond C«Primary protein structure only peptide bond hydrogen bond develop to 144 N Coiled cor xhelix C B-sheet usecondry protein structuren. @hydrogen bond develop to Globular Q CCH₃ = @aprotein 3D shape, Biological function" aTertiary protein structure» Polded Qe All types of bonds *Primary protein structure 8- -The sequence of amino acids will determine The protein shape and function. If we change the a a sequence, The shape and protein function will be altered. + Hi 20 peptide hord H H2O 入 H H H HN-C-C N-CC T T CH3 Dehydration CH2 CH2 Condensation OH SH Alanine Serine Cysteine 1-Terminall N Ala ser cys ICIC-Terminal Alanyl seryl Cysteine «Tripeptide» mean 3 residues>> Ex& Nphe cys glu C A Vie "phenylalanyl Cystyl glutamate " «Tripeptide NVal Arg ser Alac "Valyl Arginy Iserylalanine, B Tetrapeptide protein A function differs from protein B Punction. *Example of Primary protien structure :- NGlu Cys glycine C Tripeptide, Pound in ISHlumast active groupn every cell * Glutamyl Cysteinyl glycine -Glutathione GSH * Reducing agent Antioxidant 1-protect RBC membrane from H2O2 2. ↑ Amino acids absorption 3. Enzyme activation 4_Detoxification of drugs REC Glutathione + selenium + vit. E, vit. C "Antioxidants" " protection from hemolysis" * properties of peptide bond. harsh conditions 1- very strong, destroyed by heating lloc + 6m HCl for 24 hour 11 2- Trans rather than Cis configration 3_ partial double bond, shorter than single bond. 40% C N» «resonance H 4_ Polar but uncharged 5. Rigid, planar no rotation *. Enzymatic Hydrolysis of peptide bond Nlys Arg C N phe tyr Trp c Trypsin chemotrypsin Pepsin basica a 11 a Aromatic a.all. *. Secondary protein structure * Hydrogen bond "Coils, spirals, turns AI x-helix 1- Right handed is more stable 2. side chains extended outside backbone 3_Each turn 3.60.a 4- Intra chain H. bond «stability» 5.&-helix is found in a - keratin 6-Proline is x-breaker «Cause kink formation, N backbone →Intrachain H. bonds Connect each 4tha.a ④ proline * Factors disrupt a-helix: Kink ↑ 1- proline contain pyrroliditre ring that Cause kink of helix 2. Charged aas & Glu, Asp, lys, Arg, His Couses attration and repulsions ↓ 3- Bulkya.a & Tryptophan, BCAA branched chean BB-plented sheet: 2 or more polypeptides linked by inter chain hydrogen bond"> • may be formed of one polypeptide fold on itself.. +N Intra Chain H. bend C - Antiparallel Bished inter Chain Hi bond more stable - parallel B sheet Note : x-helix is Pound in globular proteins Like myoglobin, hemoglobin. side Chains alternate above and below. 12R each tum [B. sheet precipitation, amyloid protein] Alzheimers disease" Alucanumat 4 4 *- Amyloid is neurotoxic protein Cause e Neuro degeneration cause dementia A B.Turn a reverse turn or. B. bend. Secondary protein structure contarn 4 amino acids proline glycine kink" provide H. bond's>> Connect anti parallel B.sheet N CN B-Turn N-C proline & glycine B-sheet Anti parallel supersecondary on motif,