Amino acids
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What compounds do amino acids contain | show 🗑
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show | Amino acids represent building blocks for proteins, which are the most
abundant and functionally diverse molecules in the living system
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How many amino acids are coded for by DNA | show 🗑
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show | • Based on nature of their side chain groups
• Based on polarity
• Based on fate of carbon skeleton
(metabolic fate)
• Based on nutritional requirement
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show | ▪Determines the identity of different amino acids
▪Dictates the role of amino acid in a protein.
▪Determines the properties of amino acids in protein chains.
▪R –gps of certain amino acids crucial for the activity of enzymes
▪some acts as buffers.
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What different types of side chains can you get with amino acids ? | show 🗑
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show | Organic compounds whose carbon atoms are linked in open chains, either straight or branched.
Eg:Glycine, Alanine, Valine, Leucine and Isoleucine
can either be branched or unbranched
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show | Have an OH-
Eg:Serine, threonine and tyrosine
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show | Cysteine and methionine
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show | >Aspartate
>Glutamate
>Asparagine
>Glutamine
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Examples of side chains containing basic groups? | show 🗑
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show | Histidine, phenylalanine, tyrosine and tryptophan
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show | Proline
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Define non-polar | show 🗑
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show | Uneven distribution of electrons
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show | >Have no charge on R group
>hydrophobic (water hating)
> nonpolar side chain which does not gain or lose proton or participate in hydrogen or ionic bonds
> Stabilize tertiary & quaternary structure of protein by hydrophobic interactions
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Where can you find non polar amino acids? | show 🗑
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What are the distinctive properties of proline? | show 🗑
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Properties of amino acids with polar side chains? | show 🗑
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show | - attachment for Phosphate group in proteins
- Participate in hydrogen bonding in protein structure
- Attachment of carbohydrate moiety in glycoproteins
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show | > Participate in hydrogen bonding in protein structure at alkaline pH
>Active site of many enzymes
> In proteins, the –SH group of two cysteine residues can be oxidized to form a disulfide bond (-S-S-)
>Stabilization of tertiary structure of proteins
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What do the Amino acids with Amide groups do? | show 🗑
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What do charged polar amino acids help stabilise? | show 🗑
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show | > Dicarboxylic monoamino acids having negatively charged R group
>Proton donors
>At physiologic pH, the side chains of these amino acids are fully ionized containing a negatively charged carboxylate group (-COO-)
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Properties of Amino acids with basic side chains? | show 🗑
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What makes histidine different from other amino acids with basic side chains? | show 🗑
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show | >Not synthesized in the body
> Should be taken in the diet.
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What are the 10 essential Amino acids? | show 🗑
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What does non-essential amino acids mean? | show 🗑
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show | Gly, Ala, Ser, Cys, Asp, Asn, Glu, Gln, Tyr, Pro
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show | Gluogenic , Ketogenic or Glucogenic and Ketogenic
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What are the glucogenic amino acids? | show 🗑
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What are the Ketogenic amino acids? | show 🗑
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What are the glucogenic and ketogenic amino acids? | show 🗑
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What type of behaviours do all amino acids exhibit | show 🗑
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In aqueous solution what do amino acids contain? | show 🗑
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show | Each amino acid has a carboxyl group and a primary amino group (with an exception of Proline, which has a secondary amino group) and a distinctive side chain (“R group”) which is bonded to the α-carbon atom
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show | In two reversible forms: Protonated (acidic) & deprotonated (conjugate base)
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show | COOH
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What is the deprontonated (conjugate base) form of the carboxyl group | show 🗑
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show | NH2
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What is the protonated (Acid) form of the amide group | show 🗑
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What is meant by dissociation? | show 🗑
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What happens at physiologic pH (approximately 7.4) to the carboxyl group and amino group? | show 🗑
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show | >Peptide linkaged
>Are not available for chemical reaction except for hydrogen bond formation
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show | The side chains
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Key features of the 20 amino acids | show 🗑
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show | pK values
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show | “is the negative log. of dissociation constant of an acid Ka“
pKa = - log10Ka
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What is pKa defined as ? | show 🗑
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What is the pK of carboxyl groups? | show 🗑
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What is the pK of amino groups? | show 🗑
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show | histidine
>pK value of histidine is relatively closer to the pH of the most biological fluids
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Explain the buffering action of amino acids? | show 🗑
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show | >only imidazole (C3N2H4) group of histidine can act as buffer
>This is because the pK value of the imidazole group is relatively closer to the pH of the most biological fluids
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When is a peptide bond formed? | show 🗑
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Different structures of amino acid | show 🗑
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show | >Sequence of chain of amino acids
>Primary structure is decided by the gene that codes for the protein
>In a protein/ polypeptide chain there is a free N-terminal end and other is a C terminal end
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show | >Local folding of polypeptide chains into helices or sheets
>Primary structure determines the secondary structure
> Maintained by hydrogen bonding
> Has : α – helix and β – pleated sheets
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Tertiary amino acids? | show 🗑
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show | >has two or more peptide chains forming subunits.
>It is stabilized by hydrophobic bonds, H- bonds and electrostatic bonds.
?Subunits may function independently of each other or may work co- operatively. E.g., Hemoglobin.
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show | 153
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What is haemoglobin made up of | show 🗑
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show | Alteration in primary structure of a protein may result in derangement of its biological activity
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Outline the alpha helix ? | show 🗑
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show | α – keratin, Hemoglobin, myoglobin
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show | Proline, disrupts the conformation of the α- helix, producing a bend (Because the peptide bond nitrogen of proline lacks a hydrogen atom to contribute to a hydrogen bond )
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Why does Glycine not favor alpha helix of proteins? | show 🗑
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Condition that may not be favourable for alpha helix formation? | show 🗑
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show | >Form a zigzag or pleated pattern
> The peptide backbone of the β sheet is highly extended
> stability from hydrogen bonds between the C=O amide nitrogen of peptide bonds.
> H bonds are formed with adjacent peptide segments of the sheet
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Two peptide segments are placed in the same direction what is this called ? | show 🗑
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show | Anti -parallel
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Explain the loops and bends of amino acids? | show 🗑
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How many domains do polypeptides having more than 200 amino acids generally consist of | show 🗑
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Where can you find amino acids with non polar and polar side chains | show 🗑
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Example of a tertiary structure | show 🗑
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show | They are specialized group of proteins which facilitate the correct folding of proteins.
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show | Covalent → disulfide bonds
Non-covalent bonds → hydrogen bond, hydrophobic interactions, ionic bonds
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show | > Sharing of electrons between two non metals
Covalent bonds are strong. Bond energy is relatively high, considerable energy must be expended to break covalent bonds.
> Specific enzymes are needed to break these bonds.
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What are disulphide bonds? | show 🗑
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What are hydrophobic interactions? | show 🗑
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What are hydrogen bonds? | show 🗑
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What is ionic bonds? | show 🗑
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Explain the denaturation of proteins? | show 🗑
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What are the causes of denaturation? | show 🗑
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show | - Biological activity is lost
- Viscosity is increased
- Proteins become least soluble
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show |
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Created by:
RachelOayo