betasheets are a type of secondary structure and are found i

beta-sheets are a type of secondary structure and are found in every protein True False Negatively charged peptides flow through a cation-exchange chromatography column without binding. True False Separation of proteins in the first dimension of 2D gel electrophoresis is based on a protein\'s molecular weight. True False

Solution

9. False

10 TRUE

11 TRUE

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The -sheet (likewise -creased sheet) is a typical theme of general optional structure in proteins. Beta sheets comprise of beta strands (likewise -strand) assocpositive charged particles are pulled in to an negative charged strong support. On the other hand, in anion trade chromatography, adversely charged atoms are pulled in to a decidedly charged strong support.

Component

To improve official of every charged atom, the portable stage is for the most part a low to medium conductivity (i.e., low to medium salt fixation) arrangement. The adsorption of the atoms to the strong support is driven by the ionic association between the oppositely charged ionic gatherings in the example particle and in the utilitarian ligand on the support. The quality of the cooperation is controlled by the number and area of the charges on the atom and on the useful gathering. By expanding the salt fixation (for the most part by utilizing a straight salt slope) the particles with the weakest ionic collaborations begin to elute from the segment first. Atoms that have a more grounded ionic collaboration require a higher salt fixation and elute later in the inclination. The coupling limits of particle trade gums are by and large very high. This is of real significance in process scale chromatography, yet is not basic for explanatory scale partitions.