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6 multiple choice questions, help please!!! 1. As indicated by the PDB pages for 1OPF and 1MPO, what are the functions of OmpF and maltoporin?

6 multiple choice questions, help please!!!

1.    As indicated by the PDB pages for 1OPF and 1MPO, what are the functions of OmpF and maltoporin?

A.   The respective transport of small solutes and maltodextrins across the inner membrane of E. coli.

B.   The respective transport of small solutes and maltodextrins across the outer membrane of E. coli.

C.    The respective transport of small solutes and monosaccharides across the inner membrane of E. coli.

D.   The respective transport of small solutes and monosaccharides across the outer membrane of E. coli.

2.    As supported by both 1OPF and 1MPO, porin proteins are composed of which of the following structural motifs?

A.   Antiparallel beta barrels with hydrophilic hollow channels.

B.   Parallel beta barrels with hydrophilic hollow channels.

C.    Antiparallel beta barrels with hydrophobic hollow channels.

D.   Parallel beta barrels with hydrophobic hollow channels.

3.    Which of the following statements best describes the differences between OmpF (1OPF) and maltoporin (1MPO)?

A.   OmpF has a 16-stranded beta barrel and an alpha helical domain that partly occludes the center of the barrel, while maltoporin has an 18-stranded beta barrel and a beta hairpin domain that partly occludes the center of the barrel.

B.   OmpF has an 18-stranded beta barrel and an alpha helical domain that partly occludes the center of the barrel, while maltoporin has a 16-stranded beta barrel and a beta hairpin domain that partly occludes the center of the barrel.

C.    OmpF has a 16-stranded beta barrel and a beta hairpin domain that partly occludes the center of the barrel, while maltoporin has an 18-stranded beta barrel and an alpha helical domain that partly occludes the center of the barrel.

D.   OmpF has an 18-stranded beta barrel and a beta hairpin domain that partly occludes the center of the barrel, while maltoporin has a 16-stranded beta barrel and an alpha helical domain that partly occludes the center of the barrel.

4. The ligand in 1MPO is a ______, where the ______ residue of the ligand hydrophobically interacts with Tyr 6 and Tyr 41 of Chain A.

A.   tetrasaccharide; third

B.   tetrasaccharide; second

C.    pentasaccharide; fourth

D.   pentasaccharide; second

5.    Which of the following interactions is NOT involved in the binding of GIc 431 to Chain A in 1MPO?

A.   hydrogen bonds with His 113 and Arg 33

B.   ion pair with Arg 33

C.    van der Waals interaction with His 113

D.   hydrophobic interactions with Tyr 6 and Trp 420

6.    Which of the following statements is consistent with the following rendering of 1MPO: (a) Ribbons on for Chain A colored by conformation, (b) ribbons off for Chains B and C, (c) atoms & bonds on for Tyr 6, Tyr 41, Trp 74, Tyr 118, Phe 227, Trp 358, and Trp 420?

A.   These aromatic amino acids construct a hydrophobic pocket that is complementary in shape to the ligand and assist in ligand transport by simply blocking larger oligosaccharides, as there are no noncovalent interactions between these residues and the ligand.

B.   These aromatic amino acids construct a hydrophobic pocket that is complementary in shape to the ligand and assist in ligand transport by forming weak interactions with appropriately shaped oligosaccharides.

C.    These aromatic amino acids construct a polar pocket that is complementary to the polarity to the ligand and assist in ligand transport by simply blocking larger oligosaccharides, as there are no noncovalent interactions between these residues and the ligand.

D.   These aromatic amino acids construct a polar pocket that is complementary to the polarity to the ligand and assist in ligand transport by forming weak interactions with appropriately shaped oligosaccharides.

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