Globular proteins are typically constructed from several layers of secondary structure, with a hydrophobic core and a hydrophilic surface. Is this true for a fibrous protein such as keratin?
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Globular proteins are typically constructed from several layers of secondary structure, with a hydrophobic core and a hydrophilic surface. Is this true for a fibrous protein such as keratin?
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- Hemoglobin is a tetramer consisting of two α and two β chains.What level of protein structure is described in this statement?Amino acids are ionic compounds, very soluble in water. Proteins, however, which are made up of amino acids are much less soluble, and must be folded up very precisely to maximize their solubility. Why are proteins so much less soluble than the amino acids of which they are made?Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?
- What structural features does a sphingolipid have in common with proteins? Are there functional similarities?Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?Give an example of a protein containing primarily betapleated sheets. Is this a fibrous or globular protein?
- How does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein structure (the sum of all the folded protein chains)?Globular proteins are water-soluble, whereas fibrous proteins are insoluble in water. Indicate whether you expect the following amino acids to be on the surface of a globular protein or on the surface of a fibrous protein.(a) Ala (b) Glu(c) Leu (d) Phe(e) Ser (f) ValHow does sickle cell hemoglobin differ from normal hemoglobin at the fourth level of protein structure (the sum of all the folded protein chains)?
- What level of protein structure refers to corkscrews or sheets formed due to hydrogen bonding within a single polypeptide?Which dastardly proteins help polypeptides fold into an incorrect and non-functional state?Why is cysteine such an important amino acid for defining the tertiary structure of some proteins?