Amino Acids

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20 Terms

1
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alanine

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
2
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valine

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
3
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leucine

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
4
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isoleucine

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
5
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methionine

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
6
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phenylalanine

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
7
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tryptophan

  • nonpolar side chain

  • hydrophobic

  • no H-bond

<ul><li><p>nonpolar side chain </p></li><li><p>hydrophobic</p></li><li><p>no H-bond</p></li></ul><p></p>
8
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aspartate

  • polar: negatively charged

  • typically deprotonated at physiological pH

<ul><li><p>polar: negatively charged</p></li><li><p>typically deprotonated at physiological pH</p></li></ul><p></p>
9
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glutamate

  • polar: negatively charged

  • typically deprotonated at physiological pH

<ul><li><p>polar: negatively charged</p></li><li><p>typically deprotonated at physiological pH</p></li></ul><p></p>
10
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lysine

  • polar: positively charged

  • pKa 10.5

  • protonated and positively charged at physiological pH

<ul><li><p>polar: positively charged</p></li><li><p>pKa 10.5</p></li><li><p>protonated and positively charged at physiological pH</p></li></ul><p></p>
11
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arginine

  • polar: positively charged

  • pKa 12.5

  • protonated and positively charged at physiological pH

<ul><li><p>polar: positively charged</p></li><li><p>pKa 12.5</p></li><li><p>protonated and positively charged at physiological pH</p></li></ul><p></p>
12
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histidine

  • polar: positively charged

  • pKa 6.0

  • partially protonated at physiological pH

<ul><li><p>polar: positively charged</p></li><li><p>pKa 6.0</p></li><li><p>partially protonated at physiological pH</p></li></ul><p></p>
13
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serine

  • polar: uncharged

  • hydrophilic

  • not typically ionized at physiological pH

<ul><li><p>polar: uncharged</p></li><li><p>hydrophilic</p></li><li><p>not typically ionized at physiological pH</p></li></ul><p></p>
14
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threonine

  • polar: uncharged

  • hydrophilic

  • not typically ionized at physiological pH

<ul><li><p>polar: uncharged</p></li><li><p>hydrophilic</p></li><li><p>not typically ionized at physiological pH</p></li></ul><p></p>
15
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glutamine

  • polar: uncharged

  • hydrophilic

  • not typically ionized at physiological pH

<ul><li><p>polar: uncharged</p></li><li><p>hydrophilic</p></li><li><p>not typically ionized at physiological pH</p></li></ul><p></p>
16
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asparagine

  • polar: uncharged

  • hydrophilic

  • not typically ionized at physiological pH

<ul><li><p>polar: uncharged</p></li><li><p>hydrophilic</p></li><li><p>not typically ionized at physiological pH</p></li></ul><p></p>
17
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tyrosine

  • polar: uncharged

  • hydrophilic

  • not typically ionized at physiological pH

<ul><li><p>polar: uncharged</p></li><li><p>hydrophilic</p></li><li><p>not typically ionized at physiological pH</p></li></ul><p></p>
18
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glycine

  • only H atom as side chain

  • not chiral

  • can reside in sites where two polypeptides come into close contact

<ul><li><p>only H atom as side chain</p></li><li><p>not chiral</p></li><li><p>can reside in sites where two polypeptides come into close contact</p></li></ul><p></p>
19
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cysteine

  • polar, uncharged

  • can form covalent bond to make a disulfide link

<ul><li><p>polar, uncharged</p></li><li><p>can form covalent bond to make a disulfide link</p></li></ul><p></p>
20
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proline

  • hydrophobic character

  • can create kinks in polypeptide chains and disrupt secondary structure

<ul><li><p>hydrophobic character</p></li><li><p>can create kinks in polypeptide chains and disrupt secondary structure</p></li></ul><p></p>