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15 Cards in this Set
- Front
- Back
- 3rd side (hint)
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Polypeptides usually have molecular weight |
Less than 5000 |
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Proteins have molecular weight ranging from |
6000 to 40,000,000 |
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Proteins are classified into |
SCFG--- Simple, conjugated, fibrous and globular proteins |
SCFG |
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_______ proteins are folded into spherical shapes and function as Enzymes, Hormones, Transport Protein |
Globular |
EHTP |
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_______ proteins are the type that are bonded to a non protein group e.g sugar, nucleic acid or lipid. |
Conjugated |
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Define primary structure |
This means/shows the sequence of the amino acids in the chain and the location of disulfide links if any. |
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Peptide linkages are example of what type of bond? |
Covalent bond |
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A special characteristic of peptide bond is that they are? |
Partial double bond, hence they have no freedom of rotation. Although the bonds on each sides of the alpha carbon atom are free to rotate within spatial constrain. |
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Describe secondary structure of protein |
Secondary structures of protein are dependent on a non covalent interaction( hydrogen bonding) that exist between carboxyl and amino group. This results in folding of the peptide chain to either alpha helices or beta pleated sheets |
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Information about the psi and phi angles in a protein is not enough to describe the 3D structure of protein. T / F |
T |
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How are beta bends formed and stabilized? |
They are formed by abrupt u turn folding of the chain and the bends are stabilized by disulfide bridges. |
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______ have elongated structure with the polypeptide chains arranged in long strands |
Fibrous protein |
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Define quaternary structure |
This defines the conformation assumed by a multimeric protein. They are made up by several protein subunits. Joined by ionic, H and hydrophobic interactions |
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Globular proteins have more compact and often irregular structures. T or F |
T |
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Denaturation is the _________ |
Disruption of the normal structure of protein such that it loses biological activity. It is usually caused by heat or changes in pH |
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