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Date: Sun, 28 Mar 2021 06:47:23 -0700
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From: "Clogged Arteries" <CloggedArteries@proheros.biz>
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Subject: ***SPAM*** Cure High Cholesterol By Cutting Out This ONE Ingredient

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The study of proteins in vivo is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the cytoplasm and membrane-bound or secreted proteins in the endoplasmic reticulum, the specifics of how proteins are targeted to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a fusion protein or chimera consisting of the natural protein of interest linked to a "reporter" such as green fluorescent protein (GFP).[68] The fused protein's position within the cell can be cleanly and efficiently visualized using microscopy,[69] as shown in the figure opposite. Other methods for elucidating the cellular location of proteins requires the use of known compartmental markers for regions such as the ER, the Golgi, lysosomes or vacuoles, mitochondria, chloroplasts, plasma membrane, etc. With the use of fluorescently tagged versions of these markers or of antibodies to known markers, it becomes much simpler to identify the localization of a protein of interest. For example, indirect immunofluorescence will allow for fluorescence colocalization and demonstration of location. Fluorescent dyes are used to label cellular compartments for a similar purpose.[70] Other possibilities exist, as well. For example, immunohistochemistry usually utilizes an antibody to one or more proteins of interest that are conjugated to enzymes yielding either luminescent or chromogenic signals that can be compared between samples, allowing for localization information. Another applicable technique is cofractionation in sucrose (or other material) gradients using isopycnic centrifugation.[71] While this technique does not prove colocalization of a compartment of known density and the protein of interest, it does increase the likelihood, and is more amenable to large-scale studies. Finally, the gold-standard method of cellular localization is immunoelectron microscopy. This technique also uses an antibody to the protein of interest, along with classical electron microscopy techniques. The sample is prepared for normal electron microscopic examination, and then treated with an antibody to the protein of interest that is conjugated to an extremely electro-dense material, usually gold. This allows for the localization of both ultrastructural details as well as the protein of interest.[72] Through another genetic engineering application known as site-directed mutagenesis, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation. This technique even allows the incorporation of unnatural amino acids into proteins, using modified tRNAs,[73] and may allow the rational design of new proteins with novel properties

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The study of proteins in vivo is =
often concerned with the synthesis and localization of the protein within t=
he cell. Although many intracellular proteins are synthesized in the cytopl=
asm and membrane-bound or secreted proteins in the endoplasmic reticulum, t=
he specifics of how proteins are targeted to specific organelles or cellula=
r structures is often unclear. A useful technique for assessing cellular lo=
calization uses genetic engineering to express in a cell a fusion protein o=
r chimera consisting of the natural protein of interest linked to a "report=
er" such as green fluorescent protein (GFP).[68] The fused protein&#39;s po=
sition within the cell can be cleanly and efficiently visualized using micr=
oscopy,[69] as shown in the figure opposite. Other methods for elucidating =
the cellular location of proteins requires the use of known compartmental m=
arkers for regions such as the ER, the Golgi, lysosomes or vacuoles, mitoch=
ondria, chloroplasts, plasma membrane, etc. With the use of fluorescently t=
agged versions of these markers or of antibodies to known markers, it becom=
es much simpler to identify the localization of a protein of interest. For =
example, indirect immunofluorescence will allow for fluorescence colocaliza=
tion and demonstration of location. Fluorescent dyes are used to label cell=
ular compartments for a similar purpose.[70] Other possibilities exist, as =
well. For example, immunohistochemistry usually utilizes an antibody to one=
 or more proteins of interest that are conjugated to enzymes yielding eithe=
r luminescent or chromogenic signals that can be compared between samples, =
allowing for localization information. Another applicable technique is cofr=
actionation in sucrose (or other material) gradients using isopycnic centri=
fugation.[71] While this technique does not prove colocalization of a compa=
rtment of known density and the protein of interest, it does increase the l=
ikelihood, and is more amenable to large-scale studies. Finally, the gold-s=
tandard method of cellular localization is immunoelectron microscopy. This =
technique also uses an antibody to the protein of interest, along with clas=
sical electron microscopy techniques. The sample is prepared for normal ele=
ctron microscopic examination, and then treated with an antibody to the pro=
tein of interest that is conjugated to an extremely electro-dense material,=
 usually gold. This allows for the localization of both ultrastructural det=
ails as well as the protein of interest.[72] Through another genetic engine=
ering application known as site-directed mutagenesis, researchers can alter=
 the protein sequence and hence its structure, cellular localization, and s=
usceptibility to regulation. This technique even allows the incorporation o=
f unnatural amino acids into proteins, using modified tRNAs,[73] and may al=
low the rational design of new proteins with novel properties

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