Term
| What is an amino acid comprised of? |
|
Definition
r
amino group
carboxyl group
g
center=c |
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Term
| At neutral pH, most amino acids have charges on what end? |
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Definition
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|
Term
| What are the different classes of amino acids? |
|
Definition
Hydrophobic-nonpolar
Hydrophilic-basic, acidic, polar
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Term
| How do amino acids differ? |
|
Definition
Hydrophobic vs hydrophilic (intra-and inter- molecular interactions)
shape/size
unique characteristics
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Term
| What is notable about Glycine? |
|
Definition
It is small
amino acid
constricts other connections
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|
|
Term
| What is noticable about proline? |
|
Definition
it has a ring
the ring will restrict its ability to move |
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|
Term
| What is noteworthy about Methionine? |
|
Definition
First amino acid in every protein
Every cell that makes protein, starts that process with methionine |
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Term
| What is the notable between Serine, Threonine, And Tyrosine? |
|
Definition
| They have a Hydroxyl group (OH) where you can add a phosphate group |
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|
Term
| What is unique about a cysteine? |
|
Definition
| They can form a disulfide to link to another cysteine |
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|
Term
| How is a polypeptide formed? |
|
Definition
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|
Term
| What is formed by dehydration reaction that occurs in a polypeptide? |
|
Definition
|
|
Term
| What groups add to eachother in a protein? |
|
Definition
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|
Term
|
Definition
|
|
Term
|
Definition
| carboxyl end of a protein |
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|
Term
| What are the four levels of protein structure? |
|
Definition
Primary
Secondary
Tertiary
Quaternary |
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|
Term
| Is there branching in proteins? |
|
Definition
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|
Term
| What is the primary structure of a protein? |
|
Definition
Linear sequence of amino acids-length and comosition
Ultimate determinant of shape and function-Drives formation of higher level structures |
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|
Term
| What are two features of the linear sequence of amno acids? |
|
Definition
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|
Term
| What does the ultimate determinant of shape and function of proteins drive? |
|
Definition
| formation of higher level structures |
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|
Term
| Describe the secondary strucure of the protein? |
|
Definition
Localized three-dimensional structure
Results from interations along the polypeptide backbone |
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|
Term
| What are the two types of secondary structure? |
|
Definition
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|
Term
| What seperates the alpha helix from the beta sheet? |
|
Definition
alpha helix=spiral,spinning around and around pointing outwards
Beta sheet=ribbon,side by side lining up in opposide direction |
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|
Term
| What are secondary structures held by? |
|
Definition
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|
Term
| What is the tertiary structure? |
|
Definition
What you get when the secondary structre elements interact with eachother
-Refers to the shape of the entire polypeptide |
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|
Term
| What type of interactions result in forming tertiary structures? |
|
Definition
- Hydrogen bonding
- ionic bonding
- association of hydrophobic regions
- Van der Waals interaction-stacking of rings
- covalent bonding
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|
|
Term
| What is connected with covalent bonding in tertiary structures? |
|
Definition
|
|
Term
| What is the quaternary structure? |
|
Definition
| Stable interactions among multiple polypeptides |
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|
Term
| What is hemoglobin a good example of structure wise? |
|
Definition
| the quaternary structure, there are multiple groups of polypeptides, alpha and beta pairs |
|
|
Term
| What makes the transthyretin protein a unique quaternary structure? |
|
Definition
| there are four identical polypeptides |
|
|
Term
| What do protein structures allow? |
|
Definition
| allows other protein to interact |
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|
Term
| How do single amino acids effect the protein strucure? give an example |
|
Definition
A single change can cause dramatic effects
ex) sickle cell- replaceing a hydrophilic with a hydrophobic, results in misshaped hemoglobin, that can get stuck in vascular blood flow |
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|
Term
|
Definition
| how proteins are folded in order to function naturally |
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|
Term
| Is protein folding spontaneous or non spontaneous? |
|
Definition
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|
Term
| Protein folding usually masks hydrophobic or hydrophilic domains within the protein? |
|
Definition
|
|
Term
| What is protein folding often assisted by? |
|
Definition
|
|
Term
| Is the direct process of protein assistance in protein folding a direct or indirect process? |
|
Definition
| indirect- rounds of denaturation (unfolding) and renatureatinon until it folds correctly |
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|
Term
|
Definition
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|
Term
|
Definition
|
|
Term
| What is protein folding carried out by? |
|
Definition
|
|
Term
| How does a protein know a protein is misfolded? |
|
Definition
| If there are any exposed hydrophobic domains |
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|
Term
| What does a lipid contain? |
|
Definition
Carbon
Hydrogen
small amounts of Oxygen |
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|
Term
| What is the monomer/polymer of the lipid? |
|
Definition
| There are no true monomer/polymer |
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|
Term
| How are lipids grouped together? |
|
Definition
| based on their size and hydrophobic character |
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|
Term
| Do lipids have uniform linkage? |
|
Definition
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|
Term
| Describe the process that the chaperonin must take in order to fold a protein |
|
Definition
1) An unfolded polypeptide enters the cylinder from one end
2)The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide
3)The cap comes off, and the properly folded protein is released |
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|
Term
|
Definition
| They are extended amino-to-carboxyl |
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|
Term
| What kind of bonds is the polypeptide backbone made of? |
|
Definition
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