PPT-PROPERTIES OF AMINO ACIDS
Author : gabriella | Published Date : 2022-06-07
A PHYSICAL PROPERTIES Optical properties All amino acids except glycine possess optical isomers due to the presence of asymmentric carbon atom Some amino acids
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PROPERTIES OF AMINO ACIDS: Transcript
A PHYSICAL PROPERTIES Optical properties All amino acids except glycine possess optical isomers due to the presence of asymmentric carbon atom Some amino acids have a second assymmentric carbon eg isoleucine threonine. What are amino acids?. Amino acids are the building blocks of proteins.. In the body, they exist as zwitterions.. Zwitterions can behave as both an acid or a base.. Today we will:. Study . the acid-base properties of amino acids, . (Foundation Block). Dr. Ahmed Mujamammi. Dr. . Sumbul. . Fatma. Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. CHAPTER 3, Part 1 . Amino Acids and Peptides . To know the structure and naming of all 20 protein amino acids. To know the structure and properties of peptides and the particularly the structure of the peptide bond.. Stryer. Short Course. Chapter . 3. Amino Acid Structure. Alpha carbon. Sidechain. Proteins. peptides. Stereochemisty. L-amino acids. Glycine. R/S . vs. D/L. L-isoleucine. racemization. Ionization of Amino Acids. B.2. Properties of 2-amino acids . (B.2.2). Zwitterion. (dipolar) . amino acids contain both acidic and basic groups in the same molecule . therefore, are . amphoteric. in nature (capable of behaving as acids or bases). (Foundation Block). Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. Non-standard amino acids.. Derivatives of amino acids.. DR AMINA . BIOCHEMISTRY. All tissues have some capability for synthesis of:. The non-essential amino acids,. Amino acid remodeling, . and Conversion of non-amino acid carbon skeletons into amino acids and other derivatives that contain nitrogen. . 1. . Overview. The catabolism of the amino acids involves:. Removal of α-amino groups. . Breakdown of the resulting carbon skeletons.. The resulting compounds will be used to form seven intermediate products: . ). Dr. . Sumbul. . Fatma. Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. Non-standard amino acids.. Amino acids are weak . polyprotic. acids . . Neutral amino acids are (. gly. , ala, threonine ) are treated as diprotic acids .. acidic amino acids (. glu. , asp,) are treated as . triprotic. acids .. Presented . by. Ms. . P. . . H. . Giri. Department of Microbiology. Deogiri . College, Aurangabad. B.Sc. F. Y.. Semester II. Paper No. V. Basic Biochemistry. Unit 3 Proteins. Ms. . Priyanka. H. . Giri. backbone. . atoms . (see aminoAcids1). but a unique set of . side chain . atoms. It's the side chains that make the 20 amino acids different from each other. . 1. Use the three identical backbone pieces and three unique side chain pieces below to construct three amino acids in the space to the right.. imino. acid.” . Figure 5: Comparison of the secondary amino group found in proline with the primary amino group found in other amino acids such as alanine.. 2. Proline: . Proline differs from other amino acids in that its side chain and amino N form a rigid, five -member red ring structure (Figure 5). Proline, then, has a secondary (rather than a primary) amino group. It is frequently referred to as an “. Proteins are naturally-occurring biopolymers comprised of amino acids. . The biological function of proteins is inherent in their three dimensional structure.. All the information required for correct folding of the protein into its functional .
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