AMINO ACID and PEPTIDES

Home > Preview

The flashcards below were created by user RolandoBijasa on FreezingBlue Flashcards.


  1. Compound that contains both an amino group and a carboxyl group
    Amino Acid
  2. Building blocks of protein
    Amino Acid
  3. It gives the identity to amino acid
    Side chain (R)
  4. α-amino acid has an ___________ amino group attached to the carbon adjacent to the carboxyl group
    Amino group
  5. Two steroisomers to amino acid based on similarity to glyceraldehyde
    L- or D-
  6. pH when Amino Aid is zwitter ion
    neutral
  7. di-polar ionic structure with net charge 0
    zwitter ion
  8. 4 different groups attached to AA
    • -COOH (carboxyl)
    • -NH2  (amino)
    • -H 
    • -R (Side Chain)
  9. Where amino and carboxyl group are attached
    α-carbon atom
  10. Image Upload
    • 1. non ionized form
    • 2. ionized form
  11. It does not undergo process of ionization
    Side Chain
  12. NHlocated at left
    L- AA
  13. NH2 located at right
    D- AA
  14. Found in cell wall of bacteria and peptide antibiotics
    D- isomers
  15. Found in proteins
    L- isomers
  16. Properties of Amino Acid
    • 1. asymmetry/ chirality
    • 2. optical activity
  17. both have same physical properties and chemical properties but differ in direction in w/c they rotate polarized lght
    optical activity
  18. 2 isomers result because of this chiral C (L AA and D AA)
    asymmetry/ chirality
  19. example of not asymmetric AA
    Glycine
  20. have both polar and nonpolar region
    amphiphatic
  21. example of amphiphatic AA
    tyrosine
  22. Classification of AA as to structure of the side chain
    • 1. hydrophobic or non polar (aliphatic and aromatic)
    • 2. polar
  23. AA with side chains that do not like to reside in aqueous environment. These AA buried within the hydrophobic core of the protein
    Hydrophobic (Non-Polar)
  24. AA with side chains that prefer to reside in an aqueous environment and can be generally found exposed on the surface of a protein
    Polar
  25. Hydrophobic group that contains only carbon or hydrogen atoms
    Aliphatic
  26. contains aromatic ring system
    aromatic
  27. the simplest amino acid, although placed under nonpolar and aliphatic its small H do not contribute much to hydrophobic interaction
    Glycine (gly)
  28. an example of imino acid
    Proline (pro)
  29. Sulfur containing AA
    • Cysteine (Cys)
    • Methionine (Met)
  30. Image Upload
    Gly
  31. Image Upload
    Ala
  32. Image Upload
    cys
  33. Image Upload
    ile
  34. Image Upload
    leu
  35. Image Upload
    met
  36. Image Upload
    phe
  37. Image Upload
    pro
  38. Image Upload
    trp
  39. Image Upload
    tyr
  40. Image Upload
    val
  41. Image Upload
    asn
  42. Image Upload
    ser
  43. Image Upload
    gln
  44. Image Upload
    thr
  45. Image Upload
    arg
  46. Image Upload
    lys
  47. Image Upload
    his
  48. Image Upload
    glu
  49. Image Upload
    aspartate
  50. Side chain of tyr
    phenol
  51. Side chain of trp
    indole
  52. Side chain of asp
    carboxyl
  53. Side chain of arg
    guanidino
  54. Side chain of asn
    amide
  55. Side chain of cys
    thiol/ sulfhydyl
  56. Side chain of Met
    thio-ether
  57. Side chain of phe
    benzene
  58. Side chain of his
    imidazole ring
  59. Side chain of  thr
    hydroxyl
  60. Side chain of lys
    epsilon amino
  61. derived from phe by hydroxylation
    tyrosine
  62. simplest AA
    glycine
  63. S containing AA that is essential
    methionine
  64. S containing AA that is not essential
    cysteine
  65. essential for children
    Arginine
  66. gives histamine when decarboxylated
    histidine
  67. precursor of cathecolamines
    tyrosine
  68. cathecholamines
    Dopamine, Epinephrine, Norepinephrine
  69. abundant in milk
    tryptophan
  70. precursor of Serotonin, Melanin and Niacin
    tryptophan
  71. positive at pH = 7
    Lysine
  72. negative at pH = 7
    Aspartic
  73. polar
    lys, aspartic
  74. aromatic
    phe, trp
  75. will give adrenalin
    tyrosine
  76. will form dopa (precursor of dopamine)
    tyrosine
  77. inhibitory hormone
    GABA
  78. excitatory hormone
    Glutamate
  79. secreted when there is emergency
    adrenaline, noradrenaline
  80. essential amino acid
    • (PVT TIM HALL)
    • phe
    • val
    • trp
    • thr
    • ile
    • met
    • his
    • arg
    • lys
    • leu
  81. uclassifiable
    gly
  82. precursor of GABA
    glutamic acid
  83. precursor of Histamine
    histidine
  84. precursor of Dopamine
    tyrosine
  85. precursor of throxine
    thyrosine
  86. combination of two AA
    Dipeptide
  87. Function of AA
    • Synthesis of pretein
    • precursor of N-bases of nucleic acid
    • function as chemical messenger / neurotransmitter
    • glucose synthesis
    • buffer
    • detoxification reaction (gly,cys,met)
  88. neutralizes acid and base
    buffer
  89. regulates mood appetite and sleep
    Serotonin
  90. controls the sleep and wake cycle
    melatonin
  91. ketogenic AA
    Leu, lys
  92. AA in solution at certain pH are predominantly in di polar form, fully ionized but without net charge due to COO- and NH3+
    Isoelectric point
  93. the ionization constant of ionizable groups
    pK
  94. joins amino acids in proteins formed by removal of water from a carboxyl group of one amino acid and a amino group of another
    Peptide bond
  95. reaction used in peptide bond
    dehydration reaction or condensation reaction
  96. combination of 2 or more AA
    Dipeptide
  97. combination of three AA
    tripeptide
  98. many AA are joined
    Polypeptide
  99. could have thousands of AA residues
    protein
  100. covalent bonds
    • peptide
    • disulfide
  101. non-covalent bond
    • H-bond
    • hydrophobic interaction (van der waals)
    • ionic bond
  102. cut peptide bond
    protease/ peptidase
  103. all peptide bonds in proteins occur in what configuration
    trans configuration
  104. make peptide bond planar and rigid
    partial double bond character
  105. only part on peptide ionized
    N-terminal and C-terminal
  106. released by α-cells when lower blood sugar (hypoglycemic effect)
    glucagon
  107. released by β-cells when blood sugar is high (hyperglycemic effect)
    Insulin
  108. Structures of protein
    • Primary
    • Secondary
    • Tertiary
    • Quaternary
  109. includes a description of all covalent bonds (peptide and disulfide bonds) linking AA in the polypeptide chain. determines how a protein folds into unique 3D- structure
    primary (covalent)
  110. refers to stable arrangements of AA residues giving rise to recurring structural patterns. refers only in interactions of the peptide backbone
    Secondary (H-bond)
  111. Describes all aspects of 3D folding of a peptide. 3D-arrangement of all atom
    Tertiary (covalent and noncovalent)
  112. describes the arrangement in space of a protein consisting of 2 or more subunits
    Quaternary (noncovalent interactions)
  113. it determines the function of AA
    shape
  114. arrangement
    conformation
  115. Protein secondary structure
    • alpha helix
    • beta pleated sheets
    • beta turns
    • random coil
  116. a helix breaker
    Pro
  117. hydrogen bonds are parallel to the helical axis
    α-helix
  118. more stable than left handed helix
    right hand alpha helix
  119. organizes polypeptide into sheets, extended zigzag conformation of protein backbone
    β-pleated sheet
  120. Protein backbones are arranged side by side through ________
    H-bonds
  121. the side chain of β-sheets adjacent AA protrude in ______
    opposite direction
  122. β-keratin
    silk fibroin and fibroin of spider webs
  123. protein backbone of β-sheets can be either _________
    parallel or anti-parallel
  124. more stable because the H-bonds are colinear
    anti-parallel
  125. H-bonds are ________ to the backbone direction
    perpendicular
  126. core of many protein
    β-sheets
  127. reverse the direction of a polypeptide, connects the ends of two adjacent segments of antiparallel sheet
    β-turns
  128. residues often occur in β-turns
    glycine and proline
  129. connected regions of turns and loops
    Turns and Loop
  130. short region of non α and non β conformation
    turns
  131. larger stretches with no structure, often disordered. aka "random coil"
    loops
  132. Formation of domain: section of protein structure sufficient to perform a particular chemical or physical task
    Tertiary structure
  133. Highest order of monomeric protein
    Tertiary structure
  134. stabilized by weak non covalent interactions
    Tertiary structure
  135. found in interior or core
    nonpolar
  136. outside because they can interact with water
    polar
  137. each polypeptide chain in the protein is called a
    subunit
  138. Important peptides
    [EAGOV]

    • enkephalins
    • aspartame
    • glutathione
    • oxytocin
    • vasopressin
  139. naturally occuring analgesic, similar to action of opiates
    enkephalins
  140. atificial sweetener, nutrasweet
    aspartame
  141. a tripeptide, cellular reducing agent, side effect is inhibition of melanin synthesis
    glutathione
  142. uterine contraction and milk ejection
    oxytocin
  143. reduces oxidized glutathione, powerful reducing agent
    NADPH
  144. antidiuretic (antihypertensive) hormone, makes kidney retain water, regulates BP
    Vasopressin
  145. make up 15% of the cell
    Protein
  146. function of protein
    • enzymes (catalytic)
    • structural (collagen, keratin, fibroin, elastin)
    • transport and storage (Hb, albumin, Mb
    • cell signaling (insulin receptor)
    • immune protection (immunoglobulins)
    • Hormones (insulin, glucagon)
    • coordinated motion (actin, myosin)
    • special function
  147. repeating sequence of polypeptide backbone
    N-Cα-C-N-Cα-C-N-Cα-C
  148. classification of protein
    • simple
    • conjugated
  149. composed only of amino acid (albumin, histones, protamines)
    Simple protein
  150. containsa non protein group/prosthetic group
    conjugated
  151. example of conjugated protein
    • glycoproteins
    • lipoproteins
    • metalloproteins
    • phosphoprotein
    • chromoprotein
  152. protein shape is determined by ______ of AA
    sequence
  153. final shape and has the lowest free energy possible
    conformation
  154. process of unfolding the protein
    Denaturation
  155. denaturing agents
    • heat
    • pH
    • chemical compounds (alcohol, urea, acids and bases)
  156. protein turns like a spiral fibnrous proteins (hair nails, horns)
    C
  157. protein folds back on itself as in a ribbon-globular protein
    β-sheet
  158. core of many protein
    β-sheet
  159. can be parallel or anti parallel and form rigid structures with the H-bond
    β-sheet
  160. formed by a H-bond between every 4th peptide bond -C=O to N-H
    α-helix
  161. a framework for structural protens such as the hair, nails and skin
    coiled-coil shape
  162. types of protein
    • globular
    • fibrous
  163. example of globular protein
    enzymes, transport proteins, immunoglobulins, hormones, myoglobin
  164. soluble in water in water, 2° structure is a mixture of α β & loop structures
    Globular protein
  165. usually span a long distance, insoluble in water
    fibrous protein
  166. example of fibrous protein
    collagen, keratin, silk fibroin, elastin

Card Set Information

Author:
RolandoBijasa
ID:
304231
Filename:
AMINO ACID and PEPTIDES
Updated:
2015-07-19 09:18:53
Tags:
Biochemistry
Folders:
Biochemistry
Description:
Lecture 1: Amino Acid and peptides
Show Answers:

Home > Flashcards > Print Preview