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

Match the signal sequence or post-translation modification with the target

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.

The classic experiment demonstrating that reduced and denatured RNase A could refold into the native form demonstrates that _______.

What has the greatest influence on protein stability?

______________ has emerged as a technique for protein sequencing.

When a peptide bond is formed, a(n ) [1] group reacts with a carboxylate group.   In the peptide Trp─Ser─Val, valine is at the [2].   In the tripeptide Trp─Val─Phe, the N-terminal residue is [3].

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

 ________ facilitate protein folding in vivo.

The quantitation of proteins due to their absorbance at ~280 nm (UV region) is due to the large absorbtivity of the ________ amino acids.