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39 Cards in this Set
- Front
- Back
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denaturation |
A process by which the native functional structure of a molecule has been disrupted |
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disulfide bond |
A double bond between two Sulphur atoms in cysteine side chains. |
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hydrophobic interactions |
Interaction between the R groups of hydrophobic amino acids. |
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Peptide bond |
Amino acids are linked together by a specific type of bond called a peptide bond |
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Polypeptide |
A single protein chain consisting of several amino acids bonded by peptide bonds is called a polypeptide. |
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Primary structure |
The sequence of amino acids in a polypeptide |
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quarternary structure |
The spatial arrangement of two of more individual polypeptide chains known as subunits. |
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salt bridge or ionic interaction |
An electrostatic interaction between two ionic groups of opposite charge. |
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secondary structure |
The local spatial arrangement of a polypeptide backbone atoms without regard to the conformations of its substituent side chains. |
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subunit |
A single polypeptide chain that is part of a protein with quarternary structure. |
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tertiary structure |
The entire three-dimensional structure of a single chain polypeptide including the conformations of its side chains. |
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Is this amino acid polar, nonpolar or charged? Phenylalanine is shown. |
Nonpolar. Phenylalanine is a hydrophobic amino acid that contains carbon and hydrogen atoms in its R group (side chain). |
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Is this amino acid polar, nonpolar or charged? Aspartate is shown. |
Charged. |
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Is this amino acid polar, hydrophobic (nonpolar) or charged? Methionine is shown. |
Nonpolar or hydrophobic. Methionine contains mostly carbon and hydrogen atoms in its side chain, making it nonpolar. |
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Is this amino acid polar, nonpolar or charged? Tyrosine is shown. |
Polar. Tyrosine contains a OH group in the side chain that is characteristic of polar amino acids. |
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Would you most likely find this amino acid interacting with water or oil? Why? Histidine is shown. |
Water. Histidine is a polar amino and contains a NH in its R group that is characteristic of polar amino acids. |
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Would this amino acid prefer to interact with water or oil? Why? Leucine is shown.
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Oil. Leucine is a hydrophobic amino acid. |
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What feature makes cysteine a polar amino acid? An image of cysteine is provided. |
SH in the chemical structure. This is a polar covalent bond. |
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What type of bonds or interactions are responsible for the primary structure of a protein? |
Peptide bonds. |
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What are two common shapes located in the protein secondary structure? What type of bonds stabilize the secondary structure? |
alpha helices and beta-sheets. Alpha helices and beta-sheets are stabilized by hydrogen bonds. |
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When secondary structural elements in one polypeptide chain interact with one another, what is the name for this level of protein structure? What type of interactions stabilize this level of protein structure? |
Tertiary Interactions between the R groups (side chains) stabilize this level of protein structure. |
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What is the name for the level of protein structure when two or more polypeptide chains interact with one another? What interactions stabilize this level of protein structure? |
Quaternary Interactions between R groups (side chains) stabilize the quaternary level of protein structure. |
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What type of amino acids participate in hydrogen bonding? |
Polar and/or charged amino acids. |
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What type of amino acids participate in hydrophobic interactions? |
Hydrophobic (nonpolar) amino acids |
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What type of amino acids participate in ionic bonds (salt bridge)? |
charged amino acids |
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What type of amino acids participate in disulfide bonds? |
cysteine |
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Is this amino acid most likely to participate in hydrogen bonding, ionic bonds, hydrophobic interactions and/or disulfide bonds? Why? Alanine is shown. |
Hydrophobic interactions. The R group of alanine contains only carbon and hydrogen atoms. It is a hydrophobic amino acid. |
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Is this amino acid most likely to participate in hydrogen bonding, ionic bonds, hydrophobic interactions and/or disulfide bonds? Why? Serine is shown. |
Hydrogen bonding. Serine's R group (side chain) contains an oxygen atom attached to a hydrogen atom and serine is a polar amino acid. |
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Is this amino acid most likely to participate in hydrogen bonding, ionic bonds, hydrophobic interactions and/or disulfide bonds? Why? Lysine is shown. |
Ionic bonds and/or hydrogen bonds. Lysine has a charged R group (side chain). It also has a nitrogen attached to a hydrogen atom, a feature favorable in the formation of hydrogen bonds. |
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What type of interaction is shown? |
Disulfide bond |
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What type of interaction is shown? |
hydrogen bond |
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What type of interaction is shown? |
hydrophobic interactions |
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As a piece of bacon is heated in a skillet on the stove, you observe that the appearance of the bacon changes. You may even notice that the bacon becomes crispy if left in the skillet. What type of bonds or interactions in proteins are susceptible to temperature changes? Why? |
Hydrophobic interactions. As the temperature increases, as it does in the skillet, the atoms in the proteins in bacon begin to move more rapidly. This causes the hydrophobic areas of the protein to become exposed. |
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Slow-cooker recipes will occasionally call for the addition of a soda pop or cola to tenderize a pot roast. What types of bonds or interactions in proteins would most likely be disrupted by the addition of an acidic soda pop or cola? |
Hydrogen bonds and Ionic bonds in protein are both susceptible to pH changes. Soda pop or cola contains acid and this will lead to a drop in pH in the slow cooker. |
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Disulfide bonds are disrupted by __________. |
reducing agents |
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If lysine is required at position #150 in the peptide chain in order for a protein to properly fold and function, what happens if amino acid #150 is mutated or changed from lysine to alanine? The structures of lysine and alanine are provided below. |
If a positively charged amino acid like lysine is changed to a hydrophobic amino acid (alanine), the protein will not fold properly. If the protein does not fold properly, it will not function. |
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Name the hydrophobic (nonpolar) amino acids. |
Alanine Valine Phenylalanine Tryptophan Leucine Isoleucine Methionine Proline |
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Name the polar amino acids. |
Serine Threonine Tyrosine Cysteine Asparagine Glutamine Histidine Glycine |
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Name the charged amino acids. |
Lysine Arginine Aspartate Glutamate |
