Literature DB >> 1859415

Phosphorylation and dephosphorylation modulation of an inverse temperature transition.

A Pattanaik1, D C Gowda, D W Urry.   

Abstract

Poly[15(IPGVG),(RGYSLG)], where RGYSLG is a protein kinase site, was synthesized. On raising the temperature of a 5 mg/ml solution, this polypeptide undergoes an inverse temperature transition at 18 degrees C in which it folds into a contracted state by optimizing intramolecular hydrophobic interactions. Averaging the data of five experiments, phosphorylation by means of a 3':5' cyclic AMP dependent protein kinase to the extent of one phosphate in 360 residues raises the temperature of the folding transition to 32 degrees C. The shift is completely reversed on dephosphorylation by alkaline phosphatase. Phosphorylation is hereby shown to be the most potent chemical perturbation known for shifting the temperature of an inverse temperature transition, which has been shown to be an efficient mechanism for achieving chemomechanical transduction (mechanochemical coupling).

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Year:  1991        PMID: 1859415     DOI: 10.1016/0006-291x(91)90141-s

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  7 in total

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Review 7.  Temperature-Responsive Nano-Biomaterials from Genetically Encoded Farnesylated Disordered Proteins.

Authors:  Md Shahadat Hossain; Zhe Zhang; Sudhat Ashok; Ashley R Jenks; Christopher J Lynch; James L Hougland; Davoud Mozhdehi
Journal:  ACS Appl Bio Mater       Date:  2022-01-19
  7 in total

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