TLS Online TPP Program

#Question id: 11210


An inhibitory postsynaptic potential (IPSP) occurs in a membrane made more permeable to ________.

#Part-B Specialized Branches in Biotechnology
  1. potassium ions
  2. sodium ions
  3. ATP
  4. all neurotransmitter molecules
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TLS Online TPP Program

#Question id: 732

#Part-B Specialized Branches in Biotechnology

Ramachandran plots can help increase the accuracy of models derived from x-ray crystallography data. The plot below was created by measuring phi, and psi for each amino acid residue in a 2.2 A resolution crystal structure. In the plot, which excludes Gly and Pro residues, selected residues (dots) are numbered 1 through 5.

Which of the following statements can be correctly stated for this plot in reference to selected residues?

A. Residues 1 and 3 are in either B sheets

B. residue 2 is in a right-handed a helix, and residue 4 is in a left-handed a helix.

C. If residue 5 were Gly, it might be in an acceptable position in the plot

TLS Online TPP Program

#Question id: 734

#Part-B Specialized Branches in Biotechnology

Which of the following statements is true for two different tripeptides consisting of either glycine or proline?

TLS Online TPP Program

#Question id: 736

#Part-B Specialized Branches in Biotechnology

The most important contribution to the stability of a protein’s conformation appears to be the:

TLS Online TPP Program

#Question id: 738

#Part-B Specialized Branches in Biotechnology

Which of the following is correct for peptide bonds

A) C and N are shorter than typical C-N bonds.

B) C and N are longer than typical C-N bonds.

C) C and O are longer than typical C=O bonds.

D) C and O are shorter than typical C=O bonds.

TLS Online TPP Program

#Question id: 740

#Part-B Specialized Branches in Biotechnology

The conformation of the backbone of a polypeptide is described completely by the angle(s) of rotation about which bond(s)?

TLS Online TPP Program

#Question id: 742

#Part-B Specialized Branches in Biotechnology

Match the following

Conformation

Phi

Psi

Omega

A. Alpha helix

I. -57

P. -47

X. 180

B. B sheet

II. -135

Q. +135

Y. 0

C. Polyproline I

III. -83

R. +158

D. Polyproline II

IV. -78

S. +149