https://www.ets.org/s/grelpdt/practice book blochem.adf 3. Eukaryotie cells and

Question

https://www.ets.org/s/grelpdt/practice book blochem.adf 3. Eukaryotie cells and their organelles are disrupted by soeication. A centrifuge is used to separme soluble and insoluble s found in the insoluble fraction following cestrifugation. The insoluble fraction is treated with 03 M NaCI and centrifegation is repeated Prosein X is now found in the soluble fraction Proseia X would be best described as E) Outside the cell thar hey C) are encksed in cluthrin coated veicles D) are phosphorylated on mansose nesidues E) are modified by O-linked glycosylation of (A) an integral plasana membrane protein (B) an integral membeane prolein in an oganelle C) a peripheral membrane prolein The beadlike unit of droentin (D) a soluble cytoplasmic prosein E) a soluble auclear protein were is t chromatid (B) nucleosome 4. Which of the following macromolecules would C) kinelochore D) solesoid (E) scaffold ield only one type of monomer after complete A) DNA (B) Glycogen 9. Inactivation of one X chromsome in femake mammals is an example of which ofthe kilowi C) Lipoprotcis (D) RNA E Triacylelycerol (B) Sex-linked inheritance C) Autosomal dominance D) Translational control 16. Ribulose 1.3-bisphosphate carboxylase. which catalyzes the fixation of carboe dioxide during photosynthesis in plants and many algae, is first exon 13. The migration of a protcin on an SDS in which of the following cellular (A) negative charge (B) isoelectric point (C) log of carbohydrate content (D) log of molecular weight (E) native volume (A) Peroxisomes (B) Chloroplasts (C) Mitochondria (D) Lysosomes E) Plant cell vacuoles

Explanation / Answer

Chegg policy to answer the first 4 questions in the questionare : 4 MCQs with explanation are as follows:

1]Salting in refers to the effect where increasing the ionic strength of a solution increases the solubility of some solute (such as a protein).This effect tends to be observed at lower ionic strengths.[citation needed]Protein solubility is a complex function of the physicochemical nature of the protein, pH, temperature, and the concentration of the salt used. It also depends on whether the salt is kosmotropic (stabilizes water) the proteins usually increases slightly (salting in). But at high concentrations of salt, the solubility of the proteins drop sharply (salting out).Proteins are surrounded by the salt counterions (ions of opposite net charge) and this screening results in decreasing electrostatic free energy of the protein and increasing the activity of the solvent, which in turn, leads to increasing solubility.

In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure.Amphitropic proteins associate with lipid bilayers via various hydrophobic anchor structures. Such as amphiphilic -helixes, exposed nonpolar loops, post-translationally acylated or lipidated amino acid residues, or acyl chains of specifically bound regulatory lipids.These interactions can be brought down by addition of salt to salt-in these proteins in the water soluble fraction.

2]Glycogen

Glycogen is a branched biopolymer consisting of linear chains of glucose residues with an average chain length of approximately 8–12 glucose units.[14] Glucose units are linked together linearly by (14) glycosidic bonds from one glucose to the next. Branches are linked to the chains from which they are branching off by (16) glycosidic bonds between the first glucose of the new branch and a glucose on the stem chain.

3]Unique property of lysosomal enzymes:(are phosphorylated on mannose residues)

The production of lysosomal proteins suggests one method of lysosome sustainment. Lysosomal protein genes are transcribed in the nucleus. mRNA transcripts exit the nucleus into the cytosol, where they are translated by ribosomes. The nascent peptide chains are translocated into the rough endoplasmic reticulum, where they are modified. Upon exiting the endoplasmic reticulum and entering the Golgi apparatus via vesicular transport, a specific lysosomal tag, mannose 6-phosphate, is added to the peptides. The presence of these tags allow for binding to mannose 6-phosphate receptors in the Golgi apparatus, a phenomenon that is crucial for proper packaging into vesicles destined for the lysosomal system.

4]Bead-like unit of Chromatin Structure : Nucleosome

A nucleosome is a basic unit of DNA packaging in eukaryotes, consisting of a segment of DNA wound in sequence around eight[1] histone protein cores.Nucleosomes form the fundamental repeating units of eukaryotic chromatin.

DNA wraps around histone proteins forming nucleosomes; the "beads on a string" structure (euchromatin). Multiple histones wrap into a 30 nm fibre consisting of nucleosome arrays in their most compact form (heterochromatin).

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