Sandbox chaperones: Difference between revisions

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The primary function of [[Chaperones]] is protein folding. They are proteins that assist/chaperone other proteins as they fold or unfold and assemble or disassemble in order to prevent misfolding and unwanted protein aggregation.

Some chaperones function closely with ribosomes in order to help fold newly made proteins, sometimes co-translationally. However, most proteins will fold spontaneously without the help of a chaperone. Chaperones become necessary for most proteins only when the intracellular environment becomes too crowded, thus increasing the chances of protein aggregation unless aided by a chaperone.

Some chaperones function closely with ribosomes in order to help fold newly made proteins, sometimes co-translationally. However, most proteins will fold spontaneously without the help of a chaperone. Chaperones become necessary for most proteins only when the intracellular environment becomes too crowded, thus increasing the chances of protein aggregation unless aided by a chaperone. See also [[Chaperones]]

Many chaperones are heat shock proteins (typically abbreviated as "Hsp" with the approximate molecular weight afterwards) that are expressed in response to high temperatures or other cellular stresses which impact protein folding. In these environments chaperones function to prevent or correct damage caused by misfolding and to prevent unwanted protein aggregation, which is more likely to happen when proteins are denatured by stress. Some heat shock protein chaperones are present at low to moderate levels in virtually all organisms at all times in order to help in essential protein maintenance. <ref>Ellis, R.J. and van der Vies, S.M. (1991). "Molecular chaperones". Annual Review of Biochemistry 60: 321–47</ref>

Sandbox chaperones: Difference between revisions

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 The primary function of [[Chaperones]] is protein folding. They are proteins that assist/chaperone other proteins as they fold or unfold and assemble or disassemble in order to prevent misfolding and unwanted protein aggregation.
-Some chaperones function closely with ribosomes in order to help fold newly made proteins, sometimes co-translationally. However, most proteins will fold spontaneously without the help of a chaperone. Chaperones become necessary for most proteins only when the intracellular environment becomes too crowded, thus increasing the chances of protein aggregation unless aided by a chaperone.
+Some chaperones function closely with ribosomes in order to help fold newly made proteins, sometimes co-translationally. However, most proteins will fold spontaneously without the help of a chaperone. Chaperones become necessary for most proteins only when the intracellular environment becomes too crowded, thus increasing the chances of protein aggregation unless aided by a chaperone.  See also [[Chaperones]]
 Many chaperones are heat shock proteins (typically abbreviated as "Hsp" with the approximate molecular weight afterwards) that are expressed in response to high temperatures or other cellular stresses which impact protein folding. In these environments chaperones function to prevent or correct damage caused by misfolding and to prevent unwanted protein aggregation, which is more likely to happen when proteins are denatured by stress. Some heat shock protein chaperones are present at low to moderate levels in virtually all organisms at all times in order to help in essential protein maintenance. <ref>Ellis, R.J. and van der Vies, S.M. (1991). "Molecular chaperones". Annual Review of Biochemistry 60: 321–47</ref>