You have purified a new peptide hormone.  To determine its amino acid sequence you have digested the polypeptide with trypsin and in a separate reaction you have cleaved the polypeptide with cyanogen bromide.    Cleavage with trypsin yielded 5 peptides that were sequenced by Edman degradation as shown in the following.    Ser─Leu Asp─Val─Arg Val─Met─Glu─Lys Ser─Gln─Met─His─Lys Ile─Phe─Met─Leu─Cys─Arg   Cleavage with cyanogen bromide yielded 4 peptides that were sequenced by Edman degradation:   His─Lys─Ser─Leu Asp─Val─Arg─Val─Met Glu─Lys─Ile─Phe─Met Leu─Cys─Arg─Ser─Gln─Met   Determine the sequence of the intact protein.

A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly-.  The sequence is most probably part of a(n):

In general molecular chaperone proteins function by

Which one of the representations describes the oligopeptide shown below? 

Which of the following does not require ATP hydrolysis to aid in protein folding?

A protein that has had few changes in its amino acid sequence over evolutionary history is labeled

Which protein is predicted to be a membrane protein? Explain you answer. Protein A Protein B  

You are trying to separate 2 proteins by gel exclusion chromatography . Listed below is information about each protein.   Molecular Weight pI Protein 1 55 kDa 4.2 Protein 2 22 kDa 8.7 Which protein will elute first from the column? Give a reason for your choice Which other method could you use to separate this proteins? Explain

Which of the following developed during the evolution of eukaryotic cells from prokaryotic cells?

SRPs are an important part of the secretory pathway. After peptide chain elongation has paused due to binding of the SRP to the ribosome, where do SRPs dock to with their receptors?