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    20 Amino Acids

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    Joseph Paguio
    This document provides information about the 20 standard amino acids that make up proteins. It lists each amino acid's abbreviation, symbol, properties of its side chain including hydropathy index and pI value, and average frequency of occurrence in proteins. The amino acids are grouped based on the characteristics of their side chains as nonpolar, aromatic, polar uncharged, positively charged, or negatively charged. Key information about each amino acid is given, such as its single letter abbreviation, chemical structure, and how its properties influence its behavior in proteins.

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    © All Rights Reserved
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    20 Amino Acids

    Uploaded by

    Joseph Paguio
    65 views1 page
    This document provides information about the 20 standard amino acids that make up proteins. It lists each amino acid's abbreviation, symbol, properties of its side chain including hydropathy index and pI value, and average frequency of occurrence in proteins. The amino acids are grouped based on the characteristics of their side chains as nonpolar, aromatic, polar uncharged, positively charged, or negatively charged. Key information about each amino acid is given, such as its single letter abbreviation, chemical structure, and how its properties influence its behavior in proteins.

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    This document provides information about the 20 standard amino acids that make up proteins. It lists each amino acid's abbreviation, symbol, properties of its side chain including hydropathy index and pI value, and average frequency of occurrence in proteins. The amino acids are grouped based on the characteristics of their side chains as nonpolar, aromatic, polar uncharged, positively charged, or negatively charged. Key information about each amino acid is given, such as its single letter abbreviation, chemical structure, and how its properties influence its behavior in proteins.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    65 views1 page

    20 Amino Acids

    Uploaded by

    Joseph Paguio
    This document provides information about the 20 standard amino acids that make up proteins. It lists each amino acid's abbreviation, symbol, properties of its side chain including hydropathy index and pI value, and average frequency of occurrence in proteins. The amino acids are grouped based on the characteristics of their side chains as nonpolar, aromatic, polar uncharged, positively charged, or negatively charged. Key information about each amino acid is given, such as its single letter abbreviation, chemical structure, and how its properties influence its behavior in proteins.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    of 1

    - _ f

    p1(, values
    Abbreviation/
    Amino acid symbol
    Ph IKz
    M,* (-C00H) (-N$)
    Hydropathy 0ccu:rencein
    indexr proteins (%)*
    PKn
    (R group) pI
    Nonpolar, aliphatic
    R groups
    Glycine
    Alanine
    Proline
    Valine
    Leucine
    Isoleucine
    Methionine
    Aromatic
    R groups
    Phenylalanine
    $'rosine
    TYylgtophan
    Polar, uncharged
    R groups
    Serine
    Threonine
    Cysteines
    Asparagine
    Glutamine
    Gly G
    Ala A
    Pro P
    Vai V
    Leu L
    Ile I
    Met M
    Phe F
    lyr Y
    Tlp W
    Ser S
    Thr T
    Cys C
    Asn N
    Gln
    Q
    Lys K
    His H
    Arg R
    Asp D
    GIu E
    10. 53
    6. 00
    12.48
    , J. Oi )
    4.25
    75
    89
    115
    IT7
    131
    131
    149
    l 0D
    181
    204
    105
    119
    1.21.
    B2
    r46
    \ 46
    155
    \74
    133
    1 4 . 7
    2. 34
    2. 34
    1. 99
    2. 32
    2. 36
    236
    2. 28
    1. 83
    2. 20
    2. 38
    2. 21
    2. TI
    1. 96
    2.02
    2. 17
    2. r 8
    L. 82
    2. t 7
    1. 88
    2. r 9
    9. 60
    9. 69
    10. 96
    9.62
    9. 60
    9.68
    9. 2\
    9. 13
    9. 1 1
    9. 39
    9. 15
    962
    r0.28
    880
    9. r 3
    8. 95
    Lr 7
    904
    960
    967
    5. 97
    6. 01
    6.48
    5. 97
    5. 98
    6. 02
    D . t +
    -0.4
    1. 8
    1. 6
    4.2
    3. 8
    4. 5
    1 q
    2. 8
    -
    1. 3
    - 0. 9
    -0. 8
    -0.7
    9 t r ,
    - 3. 5
    7. 2
    7. 8
    5. 2
    6. 6
    9. 1
    i ). . 1
    2. 3
    3. 9
    o- a
    ) . 4
    6. 8
    5. 9
    1. 9
    +. o
    4. 2
    Z . J
    5. 1
    K A
    o..t
    5. 48
    D. 00
    5.89
    Positively charged
    R groups
    I rrqi n e
    Histidine
    Arginine
    10. 07
    818
    D. Od
    5. 87
    5.07
    5. 4r
    5.65
    9.74
    7.59
    10. 76
    2. 77
    3. 22
    _ a o
    _
    J . L
    Negatively charged
    R groups
    Aspartate
    Glutamate
    +M/val ues
    refl ect the structures as shown i n Fi gure 3-5.The el ements of water (M,78) arc del eted when the ami no aci d i s
    i ncorporated i nto a pol ypepti de.
    tA
    scal e combi ni ng hydrophobi ci ty and hydrophi l i ci ty of R groups. The val ues refl ect the free energy (AG) of transfer of the ami no
    aci d si de chai n from a hydrophobi c sol vent to water. Thi s transfer i s favorabl e (AG < 0; negati ve val ue i n the i ndex) for charged
    or pol ar ami no aci d si de charns, and unfavorabl e (AG > 0; posi ti ve val ue i n the i ndex) for ami no aci ds wi th nonpol ar or more
    hydr ophobi csi dechai ns SeeChapt er l l . Fr omKyt e, J &Dool i t t l e, R. E( 1982) Asi mpl emet hodf or di spl ayi ngt hehydr opat hi c
    character of a protei n. J. Mol . Bi ol . 157, 105- 132.
    fAverage
    occunence i n more than 1,150 protei ns. From Dool i ttl e, R.E (1989) Redundanci es i n protei n sequences.l n Predi cti on
    of Protein Structure and the Pilnciples of Protein Confornation (Fasman, G.D., ed
    ),
    pp 599-623, Plenum Press, NewYork.
    Scystei ne
    i s general l y cl assi fi ed as pol ar despi te havi ng a posi ti ve hydropathy i ndex. Thi s refl ects the abi l i ty of the sul fhydryl
    group t0 act as a weak aci d and to form a weak hydrogen bond wi th oxygen or ni trogen
    (see Fig. 1-19). All molecules
    "r/ith
    a chiral center are
    also optically active-that is, they rotate plane-
    polarized light (see Box 1-2).
    KEY C0NVENTI0N: I\.vo conventi ons are used to i denti fy
    the carbons in an amino acid-a Dractice that can be
    confusing. The additional carbons in an R group are
    commonly designated
    B , 7,6,
    E, and so forth, proceeding
    out from the a carbon. For most other organic mole-
    cules, carbon atoms are simply numbered from one end,
    giving highest priority (C-1) to the carbon with the sub-
    stituent containing the atom of highest atomic number.

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