Given the following peptide:
What would be the resulting peptides or amino acid when it is cleaved with
Leu-Arg-Asp-Phe-Ala-Lys-Met and Thr
Leu-Arg; Asp-Phe-Ala and Lys-Met-Thr
no cleavage will occur
Leu-Arg-Asp-Phe and Ala-Lys-Met-Thr
Leu-Arg-Asp-Phe-Ala and Lys-Met-Thr
Which of the following correctly describes "salting out"?
Salts compete with proteins for interactions with water which increases the solubility
of the protein
Salts form ion-dipole interactions with the protein which decreases the solubility of
Salts form ion-dipole interactions with the protein which increases the solubility of the
Salts compete with proteins for interactions with water which decreases the solubility
of the protein
What effect is seen on a Lineweaver-Burke graph when a competitive inhibitor
is added to an enzymatic reaction?
both the y-intercept and the slope change
the line is inversed
the y-intercepts changes
the slope of the line changes
neither the y-intercept nor the slope change
Considering enzyme mechanisms, what group is often attacked by
The nitrogen atom of the imidazole group.
The carbon atom of a carbonyl group.
The oxygen atom of an alcohol group.
The 3'-hydroxyl group of nucleosides and nucleotides.
The R-group of leucine.
Chymotrypsin does not work well at pH 4 because:
His57 cannot work as general base
Ser195 cannot work as nucleophile
His57 cannot work as general acid
The oxyanion would extract protons
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q2)no cleavage occur...