Term
| proteins have 7 functions |
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Definition
1. enzymes
2. defense
3. transport
4. regulation
5. structural
6. movement
7. storage |
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Term
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Definition
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Term
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Definition
| monomers...amines attached to the alpha carbon of a carboxylic acid |
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Term
| how many amino acids are there? how are they differed? |
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Definition
| 20 different kinds...by their R groups |
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Term
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Definition
| net neutral: equal positive and negative formal charges, ph 7 |
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Term
| which carbon in the amino acid is chiral? |
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Definition
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Term
| which amino acids are isolated from proteins |
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Definition
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Term
| how are amino acids classified? |
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Definition
| by the polarity of their R group |
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Term
| polar, neutral amino acids |
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Definition
| r groups that contain alcohols, thiols, and amides |
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Term
| acidic, negative amino acids |
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Definition
| r groups that contain carboxylic acids |
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Term
| basic, positive amino acids |
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Definition
| r groups that contain amines |
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Term
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Definition
| r group that are just alkyl or aryl groups (tryptophan(has amine) is nonpolar and so is methionine(has sulfur in it)) |
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Term
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Definition
| an amide bond connecting the carbonyl group of one amino acid to the amino group of the next |
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Term
| linked amino acids are called? |
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Definition
| dipeptides, tripeptides, polypeptides |
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Term
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Definition
| is the side of the amino acid chain that has the open amino group on it |
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Term
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Definition
| is the side of the amino acid chain that has the open carboxylic acid group on it |
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Term
| what is a physical property of the peptide? |
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Definition
| the bond exhibits resonance, preventing it from moving in its position, causing it to have planar geometry |
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Term
| how do you determine the primary structure of protiens? |
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Definition
the primary structure is the sequence of amino acids.
primary structure is a direct translation of the information in genes |
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Term
| how do you determine the secondary structure of proteins? |
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Definition
it is the local pattern of the chain of amino acids, and they hydrogen bond between amide hydrogen, and carbonyl together in 2 main ways 1> alpha helix, every 4th carbon
2> beta pleated sheets where they can be parallel or anti-parallel |
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Term
| secondary structure of proteins can be represented by what? |
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Definition
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Term
| how is the tertiary structure of the protein formed? |
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Definition
| it is the folding of the secondary structure,(apha helix or beta pleated sheet) it is held together through the R groups via 1. hydrophobic interactions 2. hydrogen bonds 3. ionic bonds 4. disulfide bonds |
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Term
| what are globular proteins? |
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Definition
| they are compact and spherical shaped, like a ball example: myoglobin, hemoglobin |
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Term
| what are fibrous proteins? |
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Definition
| they are long and stretched out, example:keratin, collagen |
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Term
| what is the quaternary structure of a protein? and how is it formed? |
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Definition
| it is the interactions with proteins between multiple polypeptides, same as secondary proteins> 1. hydrophobic interactions 2. hydrogen bonds 3. ionic bonds 4. disulfide bonds |
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Term
| what happens in hydrolysis of proteins? |
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Definition
| the peptide bonds in the protein are broken and it leaves the amino acids |
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Term
| what happens in denaturation of proteins? and what causes it? |
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Definition
| the weak interactions in the 2nd 3rd and 4th structures are disrupted, it is causes by high temperature, ph, and organic solvents |
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Term
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Definition
| a part of the protein that is are not amino acids like the heme in hemeglobin |
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Term
| hemoglobin structure and function? |
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Definition
| 4 polypeptide shapes, 2 alpha chains, and 2 beta chains transport oxygen to the cells |
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Term
| myoglobin structure and function? |
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Definition
| stores oxygen for muscle, and it is a globular protein made of 8 alpha helices |
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Term
| difference between sickle cell and regular hemoglobin |
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Definition
| there is a mutation in the chain of amino acids, one is deleted, and that makes more of the amino acids nonpolar, so when they touch something polar, it sickles......flattens out instead of being globular |
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