Levels Tought:
Elementary,Middle School,High School,College,University,PHD
Teaching Since: | Apr 2017 |
Last Sign in: | 234 Weeks Ago, 5 Days Ago |
Questions Answered: | 12843 |
Tutorials Posted: | 12834 |
MBA, Ph.D in Management
Harvard university
Feb-1997 - Aug-2003
Professor
Strayer University
Jan-2007 - Present
How do i figure out this answer ?
Â
You have purified a small protein. To determine its amino acid sequence you incubate the protein with trypsin and in a separate reaction you cleave the protein with cyanogen bromide.
Cleavage with trypsin yielded 5 peptides that were sequenced by Edman degradation as shown in the following.
1. Ser─Leu
2. Asp─Val─Arg
3. Val─Met─Glu─Lys
4. Ser─Gln─Met─His─Lys
5. Ile─Phe─Met─Leu─Cys─Arg
Cleavage with cyanogen bromide yielded 4 peptides that were sequenced by Edman degradation:
1. His─Lys─Ser─Leu
2. Asp─Val─Arg─Val─Met
3. Glu─Lys─Ile─Phe─Met
4. Leu─Cys─Arg─Ser─Gln─Met
What is the identity of the N-terminal amino acid in the intact protein? A. Ser
B. His
C. Asp
D. Glu
E. Ile
-----------