(3) True or False, and make correction if false I1.5 Fibroin is a ß-sheet protei

Question

(3) True or False, and make correction if false I1.5 Fibroin is a ß-sheet protein, with a high proportion of glyc of two left-handed polypeptide chains. The interactions that stabilize multisubunit complexes are different to those that stabilize tertiary structure. (4) C A) An a helix has 3.6 residues per turn. B) A network of main-chain hydrogen bonds connect ß strands in a B sheet. C) The most common structures are the ? helix and the coil structure. D) The 310 helix is right-handed and often contains proline residues E) The ? strands can be in either parallel or antiparallel configuration. ) In considering protein secondary structure which of the following are true? (Check all ap plied) [I)

Explanation / Answer

Ans 3)

True – Fibroin is an insoluble protein that is present in silk that is created by the spiders. It consists of layers of anti-parallel beta sheets and has high glycine content. The glycine content allows tight packing of the sheet and helps in giving rigid structure and tensile strength.

False- The molecule is a three left handed procollagen that join to form right handed triple helical tropocollagen. It has three polypeptide chains that are coiled around each other.

False – There are similar interactions that take place in stabilizing the multiple subunit complexes which are different from the tertiary structure.

Ans 4)

All of them are correct except for (d) The 310 helix is right handed and often contain proline residues. Rest all of them are true as the alpha helix has 3.6 residues at every turn. The two most common secondary structures are alpha helix and beta sheets that are connected by main chain hydrogen bonds. The beta sheets are most parallel or anti-parallel configuration.

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