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    <TD height=3D60 width=3D160>&nbsp;&nbsp;<A=20
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href=3D"http://www.web-books.com/MoBio/">MoBio</A><BR>&nbsp;&nbsp;<A=20
      =
href=3D"http://www.web-books.com/MoBio/Free/Contents.htm">Contents</A> =
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    <TD align=3Dmiddle height=3D60><B><FONT color=3D#008080 size=3D4>The =
Twenty Amino=20
      Acids of Proteins</FONT></B></TD></TR>
  <TR>
    <TD bgColor=3D#ff9900 height=3D30 width=3D160><A=20
      href=3D"http://www.web-books.com/MoBio/Free/Chap2.htm"><B>Chapter=20
    2</B></A></TD>
    <TD align=3Dmiddle bgColor=3D#ff9900 height=3D30><A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch2A.htm">A</A> | <A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch2B.htm">B</A> | <A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch2C.htm">C</A> | <A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch2D.htm">D</A> | <A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch2E.htm">E</A> | <A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch2F.htm">F</A> | <A=20
      =
href=3D"http://www.web-books.com/MoBio/Free/Ch2G.htm">G</A>&nbsp;</TD></T=
R></TBODY></TABLE></CENTER></DIV>
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      &nbsp;</TD>
    <TD vAlign=3Dtop><BR>
      <P>Based on the physicochemical properties of R groups, the 20 =
amino acids=20
      of proteins may be classified as follows.</P>
      <P><FONT color=3D#008080>1. Acidic:</FONT> including aspartic acid =

      (aspartate) and glutamatic acid (glutamate).&nbsp; In a neutral =
solution,=20
      the R group of an acidic amino acid may lose a proton and become=20
      negatively charged.</P>
      <P><FONT color=3D#008080>2. Basic:</FONT> including lysine, =
arginine and=20
      histidine.&nbsp; In a neutral solution, the R group of a basic =
amino acid=20
      may gain a proton and become positively charged.&nbsp; Interaction =
between=20
      positive and negative R groups may form a <B>salt bridge, =
</B>which is an=20
      important stabilizing force in proteins.</P>
      <P><FONT color=3D#008080>3. Aromatic:</FONT> including tyrosine, =
tryptophan=20
      and phenylalanine.&nbsp; Their R groups contain an aromatic=20
ring.&nbsp;</P>
      <P><FONT color=3D#008080>4. Sulfur:</FONT> including cysteine and=20
      methionine. Their R groups contain a sulfur atom (S).&nbsp; The <A =

      href=3D"http://www.web-books.com/MoBio/Free/Ch2A3.htm">disulfide =
bond</A>=20
      formed between two <B>cysteine</B> residues provides a strong =
force for=20
      stabilizing the globular structure.&nbsp; A unique feature about=20
      <STRONG>methionine</STRONG> is that the synthesis of all peptide =
chains=20
      starts from methionine (<A=20
      href=3D"http://www.web-books.com/MoBio/Free/Ch5C1.htm">Chapter 5 =
Section=20
      C</A>).</P>
      <P><FONT color=3D#008080>5. Uncharged hydrophilic:</FONT> =
including serine,=20
      threonine, asparagine and glutamine.&nbsp; Their R groups are =
hydrophilic=20
      and capable of forming hydrogen bonds.</P>
      <P><FONT color=3D#008080>6. Inactive hydrophobic:</FONT> including =
glycine,=20
      alanine, valine, leucine and isoleucine.&nbsp; These amino acids =
are more=20
      likely to be buried in the protein interior.&nbsp; Their R groups =
do not=20
      form hydrogen bonds and rarely participate in chemical =
reactions.</P>
      <P><FONT color=3D#008080>7. Special structure:</FONT> including=20
      proline.&nbsp; In most amino acids, the R group and the amino =
group are=20
      not directly connected.&nbsp; Proline is the only exception among =
20 amino=20
      acids found in protein.&nbsp; Due to this special feature, proline =
is=20
      often located at the turn of a peptide chain in the =
three-dimensional=20
      structure of a protein.</P>
      <P>&nbsp;</P>
      <P><A name=3DFigure><FONT color=3D#008080>Figure</FONT></A> <FONT=20
      color=3D#008080>2-A-2.</FONT> &nbsp;Names, symbols, chemical =
structures and=20
      hydrophobicity indices of the 20 amino acids found in =
proteins.&nbsp; They=20
      are arranged in the order as discussed above.</P>
      <P align=3Dcenter><IMG border=3D0 height=3D700=20
      src=3D"http://www.web-books.com/MoBio/Free/images/Ch2A2a.gif" =
width=3D507></P>
      <P align=3Dcenter><IMG border=3D0 height=3D665=20
      src=3D"http://www.web-books.com/MoBio/Free/images/Ch2A2b.gif" =
width=3D510></P>
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      src=3D"http://www.web-books.com/MoBio/Free/images/Ch2A2c.gif" =
width=3D516>=20
      <P><B>Note:</B> The hydrophobicity index tells the relative =
hydrophobicity=20
      among amino acids.&nbsp; More positive value indicates stronger=20
      hydrophobicity.&nbsp; Hydrophilic amino acids have negative =
values.&nbsp;=20
      In a protein, hydrophobic amino acids are more likely to be =
located in the=20
      protein interior, whereas hydrophilic amino acids are more likely =
to face=20
      the aqueous environment.</P>
      =
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Cgo=

------=_NextPart_000_00D4_01C3E02A.A2DCBF50--
