Term
| With respect to their structure, what are the most diverse class of molecules known? |
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Definition
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Term
| Proteins can serve diverse functions in cells because they are diverse in what? |
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Definition
| Size and shape as well as in the chemical properties of their amino acids. |
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Term
| A proteins underlying structure can be broken down into just four basic levels of organization, what are they? |
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Definition
| Primary, Seconday, Tertiary, Quarternary |
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Term
| Who discovered that every protein has a unique sequence of amino acids? |
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Definition
| Frederick Sanger - 1940's - 1950's |
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Term
| The unique sequence of amino acids in a protein is called... |
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Definition
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Term
| The R-groups present on each amino acid affect... |
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Definition
| its solubility and chemical reactivity. |
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Term
| These structures are distinctively shaped by sections of proteins that are stabilized largely by hydrogen bonding that occurs between the carboxyl oxygen of one amino acid residue and the hydrogen on the amino group of another |
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Definition
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Term
| Is secondary structure created between side chains or within the individual chain? |
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Definition
Individual chain!
(look at page 54)! |
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Term
| In secondary structure, hydrogen bonding between sections of the backbone is only possible when? |
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Definition
| When different parts of the same polypeptide bend in a way that puts the carboxyl groups and the amino groups close together. |
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Term
| When talking about Secondary Structure, what are two of the most important configuations that allow the formation of hydrogen bonds? |
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Definition
1. α (Alpha) Helix
2. β (Beta) pleated sheet |
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Term
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Definition
| When the polypeptide's backbone is coiled |
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Term
| What is a β-pleated sheet? |
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Definition
| When segments of a peptide chain bend 180° and then fold in the same plane. |
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Term
| When segments of a peptide chain bend 180° and then fold in the same plane. |
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Definition
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Term
| When the polypeptide's backbone is coiled |
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Definition
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Term
| The type of secondary structure that forms depends on what? |
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Definition
| The protiens primary structure. |
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Term
| Hydrogen bonds in an α-helix and a β- pleated sheet are very weak relative to covalent bonding, what then makes these structures so stable? |
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Definition
| The large amount of Hydrogen bondings. |
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Term
| The overall three-dimensional shape of a single polypeptide chain. |
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Definition
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Term
| The tertiary structure of a polypeptide results from what? |
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Definition
| The interactions between R-groups or between R-groups and the peptide backbone. |
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Term
| How many types of interactions that involve side chains are important in reguards to Tertiary Structure? |
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Definition
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Term
1st important type of interaction...Hydrogen bonds form in several ways. (In Tertiary Structure)
What are they? |
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Definition
Between hydrogen atoms and the carboxyl group in the peptide-bonded back bone
and
between hydrogen and atoms with partial negitive charges in side chains
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Term
2nd important type of interaction... What is a van der Waals interaction?
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Definition
| weak electrical attractions (weaker then hydrogen bonding) |
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Term
2nd important type of interaction... What is a van der Waals interaction?
Pt 2
How does this result in a significant increase in stability? |
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Definition
| A large number of van der Waals interactions can occur in a polypeptide when many hydrophobic residues congregate. |
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Term
| 3rd important type of interaction... disulfide bonds can form. What are these? |
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Definition
When 2 R-groups contain Sulfer, such as in cysteine, the sulfer atoms covalently bond.
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Term
In Tertiary Structure, what is frequently referred to as a bridge?
and why? |
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Definition
Disulfide Bonds.
Because they create a strong link between distinct regions of the same polypeptide. |
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Term
4th important type of interaction... well you have had the other 3, what is the last one?
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Definition
Ionic Bonding can occur between groups that have full and opposing charges.
(Ionic Bonding: metal and nonmetal through electrostatic attraction) |
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Term
| The type of tertiary structure depends on what? |
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Definition
| The primary and secondary structure! |
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Term
| What is a Quarternary Structure? |
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Definition
| The combination of polypeptide sub units.(Multiple Polypeptides) |
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Term
| Proteins with two polypeptide sub units are called what? |
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Definition
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Term
| Proteins with four polypeptide sub units are called what? |
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Definition
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Term
| remember the ten prefixes... not that you will need to know mono. |
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Definition
mono
di
tri
tetra
penta
hexa
hepta
octa
nona
deca |
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