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20 Cards in this Set
- Front
- Back
Aspartic acid |
Polar, Charged, Hydrophilic side chains act as a acid which tend to be fully charged (-) under physiologic conditions. Side chains form ionic bonds and are often involved in chemical reactions. |
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Glutamic acid |
Polar, Charged, Hydrophilic side chains act as a acid which tend to be fully charged (-) under physiologic conditions. Side chains form ionic bonds and are often involved in chemical reactions. |
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Lysine |
Polar, Charged, Hydrophilic side chains act as a base which tend to be fully charged (+) under physiologic conditions. Side chains form ionic bonds and are often involved in chemical reactions. |
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Arginine |
Polar, Charged, Hydrophilic side chains act as a base which tend to be fully charged (+) under physiologic conditions. Side chains form ionic bonds and are often involved in chemical reactions. |
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Histidine |
Polar, Charged, Hydrophilic side chains act as a base which tend to be fully charged (+) under physiologic conditions. Side chains form ionic bonds and are often involved in chemical reactions. |
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Serine |
Polar, Uncharged, Hydrophilic side chains tend to have partial charge allowing them to participate in chemical reactions, from H-bonds, and associate w/ water. |
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Threonine |
Polar, Uncharged, Hydrophilic side chains tend to have partial charge allowing them to participate in chemical reactions, from H-bonds, and associate w/ water. |
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Glutamine |
Polar, Uncharged, Hydrophilic side chains tend to have partial charge allowing them to participate in chemical reactions, from H-bonds, and associate w/ water. |
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Asparagine |
Polar, Uncharged, Hydrophilic side chains tend to have partial charge allowing them to participate in chemical reactions, from H-bonds, and associate w/ water. |
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Tyrosine |
Polar, Uncharged, Hydrophilic side chains tend to have partial charge allowing them to participate in chemical reactions, from H-bonds, and associate w/ water. |
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Alanine |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Valine |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Leucine |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Isoleucine |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Methionine |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Phenylalanine |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Tryptophan Properties? |
Nonpolar, Hydrophobic side chain consists almost entirely of C and H atoms. These A.A. tend to form the inner core of soluble proteins, buried away from the aqueous medium. They play an important role in membranes by associating with the lipid bilayer. |
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Glycine Properties? |
Side chain consists only of hydrogen atom and can fit into either a hydrophilic or hydrophobic environment. Often resides at sites where two polypeptides come into close contact. |
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Cysteine Properties? |
Though side chain has polar, uncharged character, it has the unique property of forming a covalent bond w/ another cysteine to form a disulfide link. |
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Proline Properties? |
Though side chain has hydrophobic character, it has the unique property of creating kinks in polypeptide chains and disrupting ordered secondary structure. |