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Investigation of Ph...
Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics
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- Sieradzan, Adam K. (författare)
- Univ Gdansk, Fac Chem, PL-80308 Gdansk, Poland.,Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA.
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- Korneev, Anatolii (författare)
- Far Eastern Fed Univ, Pacific Quantum Ctr, Vladivostok 690922, Russia.
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- Begun, Alexander (författare)
- Far Eastern Fed Univ, Pacific Quantum Ctr, Vladivostok 690922, Russia.
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Kachlishvili, Khatuna (författare)
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- Scheraga, Harold A. (författare)
- Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA.
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- Molochkov, Alexander (författare)
- Far Eastern Fed Univ, Pacific Quantum Ctr, Vladivostok 690922, Russia.
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- Senet, Patrick (författare)
- Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA.;Univ Bourgogne Franche Comte, Lab Interdisciplinaire Carnot Bourgogne, UMR 6303, CNRS, F-21078 Dijon, France.
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- Niemi, Antti J. (författare)
- Uppsala universitet,Stockholms universitet,Nordiska institutet för teoretisk fysik (Nordita),Far Eastern Federal University, Russia; Université de Tours, France; Beijing Institute of Technology, P. R. China,Teoretisk fysik,Far Eastern Fed Univ, Pacific Quantum Ctr, Vladivostok 690922, Russia.;Univ Tours, Lab Math & Phys Theor, CNRS, UMR 6083,Federat Denis Poisson, F-37200 Tours, France.;Stockholm Univ, NORDITA, SE-10691 Stockholm, Sweden.;Beijing Inst Technol, Sch Phys, Beijing 100081, Peoples R China.
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- Maisuradze, Gia G. (författare)
- Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA.
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Univ Gdansk, Fac Chem, PL-80308 Gdansk, Poland Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA. (creator_code:org_t)
- 2021-04-28
- 2021
- Engelska.
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Ingår i: Journal of Chemical Theory and Computation. - : American Chemical Society (ACS). - 1549-9618 .- 1549-9626. ; 17:5, s. 3203-3220
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- Apart from being the most common mechanism of regulating protein function and transmitting signals throughout the cell, phosphorylation has an ability to induce disorder-to-order transition in an intrinsically disordered protein. In particular, it was shown that folding of the intrinsically disordered protein, eIF4E-binding protein isoform 2 (4E-BP2), can be induced by multisite phosphorylation. Here, the principles that govern the folding of phosphorylated 4E-BP2 (pT37pT46 4E-BP2(18-62)) are investigated by analyzing canonical and replica exchange molecular dynamics trajectories, generated with the coarse-grained united-residue force field, in terms of local and global motions and the time dependence of formation of contacts between Cas of selected pairs of residues. The key residues involved in the folding of the pT37pT46 4E-BP2(18-62) are elucidated by this analysis. The correlations between local and global motions are identified. Moreover, for a better understanding of the physics of the formation of the folded state, the experimental structure of the pT37pT46 4E-BP2(18-62) is analyzed in terms of a kink (heteroclinic standing wave solution) of a generalized discrete nonlinear Schrodinger equation. It is shown that without molecular dynamics simulations the kinks are able to identify not only the phosphorylated sites of protein, the key players in folding, but also the reasons for the weak stability of the pT37pT46 4E-BP2(18-62).
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- NATURVETENSKAP -- Fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
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