Intrinsically Disordered Protein: Difference between revisions
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By some estimates, about 10% of all proteins are fully disordered, and about 40% of eukaryotic proteins have at least one long (>50 amino acids) disordered loop<ref name="tompa2002" />. Such sequences, under physiological conditions ''in vitro'', display physicochemical characteristics resembling those of random coils. They possess little or no ordered structure, having instead an extended conformation with high intra-molecular flexibility, lacking any tightly packed core. | By some estimates, about 10% of all proteins are fully disordered, and about 40% of eukaryotic proteins have at least one long (>50 amino acids) disordered loop<ref name="tompa2002" />. Such sequences, under physiological conditions ''in vitro'', display physicochemical characteristics resembling those of random coils. They possess little or no ordered structure, having instead an extended conformation with high intra-molecular flexibility, lacking any tightly packed core. | ||
Many [[X-ray crystallography|crystallographic]] structures have missing loops -- that is, ranges of amino acids with no [[atomic coordinate file|atomic coordinates]] in the model. These "gaps" in the model are often thought to be artifacts of inadvertant disorder in the crystal. In some cases, these gaps may be alerting us to the presence of intrinsically disordered loops in an otherwise folded protein. Such gaps are the basis for the [[#Protein disorder predictors|DISOPRED2 disorder prediction server]]. [[FirstGlance in Jmol]] offers [[Temperature_value#Missing_Residues|one method for locating and visualizaing such gaps]]. | Many [[X-ray crystallography|crystallographic]] structures have missing loops -- that is, ranges of amino acids with no [[atomic coordinate file|atomic coordinates]] in the model. These "gaps" in the model are often thought to be artifacts of inadvertant disorder in the crystal. In some cases, these gaps may be alerting us to the presence of intrinsically disordered loops in an otherwise folded protein<ref name="IDSG" />. Such gaps are the basis for the [[#Protein disorder predictors|DISOPRED2 disorder prediction server]]. [[FirstGlance in Jmol]] offers [[Temperature_value#Missing_Residues|one method for locating and visualizaing such gaps]]. | ||
Despite the existence of compelling evidence for IUPs and intrinsically disordered loops beginning in 1990<ref name="struhl1990" /><ref>PMID: 2236048</ref><ref>For the ''unstructured domain'' interpretation of early work by Pontius and Berg, see the 2004 review by Tompa and Csermley, PMID: 15284216</ref>, many current textbooks of biochemistry and even some monographs on protein structure fail to mention intrinsic disorder and its importance for protein function<ref>PMID: 18831774</ref><ref>Martz, E. Book review of <i>Introduction to protein science—architecture, function, and genomics: Lesk, Arthur M.</i>. <i>Biochem. Mol. Biol. Educ.</i> 33:144-5 (2006). [http://dx.doi.org/10.1002/bmb.2005.494033022442 DOI: 10.1002/bmb.2005.494033022442]</ref>. In 2011, Chouard provided a readable and informative overview of IUPs and how some of them function<ref>PMID: 21390105</ref>. | Despite the existence of compelling evidence for IUPs and intrinsically disordered loops beginning in 1990<ref name="struhl1990" /><ref>PMID: 2236048</ref><ref>For the ''unstructured domain'' interpretation of early work by Pontius and Berg, see the 2004 review by Tompa and Csermley, PMID: 15284216</ref>, many current textbooks of biochemistry and even some monographs on protein structure fail to mention intrinsic disorder and its importance for protein function<ref>PMID: 18831774</ref><ref>Martz, E. Book review of <i>Introduction to protein science—architecture, function, and genomics: Lesk, Arthur M.</i>. <i>Biochem. Mol. Biol. Educ.</i> 33:144-5 (2006). [http://dx.doi.org/10.1002/bmb.2005.494033022442 DOI: 10.1002/bmb.2005.494033022442]</ref>. In 2011, Chouard provided a readable and informative overview of IUPs and how some of them function<ref>PMID: 21390105</ref>. | ||
