Term
| True or false: Proteins come in all shapes and sizes |
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Definition
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Term
| What are proteins composed of? and how many? |
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Definition
| the are composed of 30 to 10,000 amino acids |
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Term
| True or false: proteins can be only globular or fibrous |
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Definition
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Term
| Broadly, What are the four shapes of proteins? |
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Definition
| Filaments, Sheets, Rings, and Spheres |
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Term
| What is protein shape specified by? |
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Definition
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Term
| For our class example in the powerpoints, proteins are assembled by how many amino acids? lecture 9 slide 3 |
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Definition
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Term
| what bond do amino acids use to bond to eachother, to form proteins? |
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Definition
| The amino acids are linked covalently by peptide bonds |
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Term
| how are covalent peptide bonds formed? |
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Definition
| they are formed between amino acids through dehydration reactions |
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Term
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Definition
| Polypeptides are chains of amino acids, The amino acids are linked covalently by peptide bonds, Proteins are made up of one or more polypeptide molecules. |
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Term
| amino acid sequence of proteins vs. nucleotide sequence of DNA |
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Definition
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Term
| Like DNA, what kind of backbone do proteins have? |
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Definition
| a polypeptide backbone, Proteins are made up of one or more polypeptide molecules. |
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Term
| Structurally, what do all amino acids have in common? |
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Definition
| all amino acids have a common base with a carboxyl terminus (COOH), and an amino terminus (NH2) |
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Term
| Structurally, how do all amino acids differ from each other? |
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Definition
| they differ by their 'side chains' or 'R-groups' |
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Term
| there are three types of non-covalent bonds that help form the 3-D shape of proteins, what are they? |
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Definition
| hydrogen bonds, electrostatic attractions, van der Waals |
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Term
| what participates in non-covalent bonding that give proteins their 3-D shape? |
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Definition
| the side chains of amino acids, the R-groups |
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Term
| non-covalent bonding strength... |
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Definition
| each of these bonds are weak, but many of these bonds together are relatively strong |
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Term
| proteins in a polar enviornment (e.g. cytoplasm) tend to have: |
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Definition
| polar side groups on the exterior of the protein (with non-polar group amino acids in the interior) |
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Term
| proteins in a non-polar enviornment (e.g. lipid bilayer) tend to have: |
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Definition
| non-polar groups on the exterior of the protein (with polar amino acids in the interior) |
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Term
| proteins fold into specific 3-D shapes based on: |
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Definition
| Their amino acid sequences |
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Term
| based on their amino acid sequence, proteins tend to form 3-D structures where |
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Definition
| the free energy is minimized (i.e. the most energetically stable configuration) |
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Term
| minor changes to protein shape are possible, depending on the two factors (both are key to a protein’s function): |
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Definition
1. the protein’s environment
2. the molecule(s )that the protein interacts with |
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Term
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Definition
| form from improper folding of a protein |
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Term
| aggregating proteins are the underlying reason for |
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Definition
| several diseases, including Alzheimer’s and Huntington’s disease, bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jacob disease (CJD) |
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Term
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Definition
assist in correct protein folding;
specifically, they provide a localized environment that allow proteins to fold properly |
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Term
| even though each protein is unique, two common folding patterns exist within each 3-D shape: |
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Definition
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Term
| what are (α-helix) and (β-sheet) folds due to? |
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Definition
| the backbone, not the R-groups |
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Term
| True or False: Proteins have similar folding patters |
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Definition
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