University:
Boston University
Course:
GMS MI 823 | Special Topics in Microbiology
Academic year:

2022
Views:

283

Pages:

45
Author:

5CelestialChronicle

Protein chemistry Biologica Catalysis Transport Storage struct 00000 →Organic compound →Are polymer of amine: acids a.a, ant building block basic unite for proteins 1804- joined by peptide bond peptide bond Anide linkage" → Covalent & strong • In trans form Partial double bond whas no free rotations Biological roles of protein.. 2 catalysis enzymes. Transport Hemoglobin... Storage Myoglobin... structure collagen a 3 protection Antibodies Regulation vhormones *Note There is no storage form for pratein in body * Structure of amino acids * More than 300 different a.ar in nature Only 20 a.ar are compose of human protein "Standard a.a,» *Each a.as consist of.. I & Carbon 3a amino group carboxylic acid 4 Hydrogen H HN-C-COOH R Chiral carbon Asymmetric carbon, ⑤ Side chain R, [Distinguish one a.a from another] * Amino acid classificati Chemical classification polarity Nor polar Polar "unchorged, acidic & basic. Nutritional classification A Essential a.a, Non essential a.a. Semi-essential Metabolic classification A Glucogenic a.as ketogenic a.a Both Glucogenic & ketogenic chemical classification. 14) A non Polar 1iglycine (Gly) 2)L-atani (Ala) EVALI "Branched a as "The smallest a as *No chiral carbon "No optical activity 4)1-leucing (Leu) 5JL-soleucine [ILE 5L-proine (pro) Branched aas *Branched a.at Thas a secamlary amo *is side chun andamine form agit five member ong stratture els cyclic a-a 771-phenylalanin (phe) aromatic shave phenyl ringu "in body it produce other a as which is tyrosin COCH 8JL-Tryptophane [Trp *aromatic "it has an Indal ring in body it produce vit.B3(niacin) SJL-methionin (Met) sulfer Containing a a (thial group) "in body it produce other aas which is cysteine Note →→Glycine, alanine & valine have a sweet taste Ⓑ pelar side chain ①Amino acids with uncharged polar si →These a.a. have zero net charge can make hydrogen bond & have inside chaim OH, SHar NH aas with OH in side chain (Sev) 211-themaning [The 3-tyrosine aromafie *porduced From phenylalanine a.as with NH2(amide) in side chain 1)-asparaging (Asn) 211-glutamine (Gin) Alas with SH in side chain 1)L-cysteine (Cys) Note 2 cysteine connecting by disulfied bond producing cystine cystine is not sulfer containing qia it is dipeptide of cysteine linked by disulfid bond →ionized "negative charge. 11-Aspartic acid (aspartate): (Asp) H CH, OH CH 2)1-glutamic acid (ghitamate): (GU) "acidic alat acidic a as Note 3-D Glutamate & Aspartate Contain dicarboxy. 2 Asparagine direved from aspartate "Asparagine is the amide of aspartate... Golatamine is THN-C-COO 1 OH amide of Glutamate CH CH2 Amino acids with basic side chain. ionized positive charge 1)L-arginini (Arg) 2)L-histidine (His) 3)L-lysine (Lys) *has guanido group *has imidazole ring *found in hemoglobin and myoglobin * amino group (epsilon) 2 Nutritional clas. A Essential a.a.: →Can not be synthesized by the body valine Threonine Histidine Arginine phenylalanine PVT TIM HALL. Tryptophan Methionine Iroleucine 1 lysine leucine Branched Valine, leucine, Isoleucine 2 Aromatic Tryptophan, phenylalanine 3 Basic Histidine, Arginine, Lysine 4 Sulfer containing Methionine 5 Threonine Non essential a.a.: Can be synthesized in sufficient amount in body Semi-essential a.a.: →Histidine & Arginine → Are essentral for infant & children, recovery from illness and pregnant women Non essential for adult Metabolic classification A Glucogenic a.as Glucose B ketogenic a.as ketone bodies imp Leucine & Lysine ketogenic & glucogenic Produce glucose & ketone bodies phomylalamine, tryptophan, tyrosine andisoleucing Note.. The brain use to glucose ketone bodies bec. it can cross as alternative fuel BBB Side chain determin characters & chemical properties of each a.Q Human bodies. can just 20 a.a, bec. they use in protein synthesis. the only aa, that human have these a genatic code Known as in DNA •Protenogenic aras 41 Protein formed by Replication Transcription 3 Translation