Structure and stability of the insulin dimer investigated by molecular dynamics simulation

Journal of Biomolecular Structure & Dynamics
M FalconiA Desideri

Abstract

Molecular dynamics simulation indicates that the dynamical behaviour of the insulin dimer is asymmetric. Atomic level knowledge of the interaction modes and protein conformation in the solvation state identifies dynamical structures, held by hydrogen bonds that stabilize, mainly in one monomer, the interaction between the chains. Dynamic cross-correlation analysis shows that the two insulin monomers behave asymmetrically and are almost independent. Solvation energy, calculated to evaluate the contribute of each interface residue to the dimer association pattern, well compares with the experimental association state found in protein mutants indicating that this parameter is an important factor to explain the association properties of mutated insulin dimers.

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Citations

May 29, 2008·Doklady. Biochemistry and Biophysics·M I DyukovO I Kiselev
Nov 22, 2005·Biophysical Journal·Patrick F DillonCharles M Lieder
Sep 1, 2005·Biophysical Chemistry·F S LeggeI Yarovsky
May 21, 2016·The Journal of Physical Chemistry. B·Xin-Xing ZhangAndrei Tokmakoff
Nov 5, 2016·International Journal of Biological Macromolecules·Hossein SoleymaniParvaneh Maghami
Nov 23, 2016·The Journal of Biological Chemistry·Krystel El HageMichael A Weiss
Mar 3, 2019·The Journal of Chemical Physics·Puja BanerjeeBiman Bagchi
Aug 14, 2008·The Journal of Physical Chemistry. B·Nevena TodorovaIrene Yarovsky
Feb 27, 2009·The Journal of Physical Chemistry. B·Nevena TodorovaIrene Yarovsky
Jan 24, 2012·Analytical Chemistry·Shigeki YamamotoPetr Bouř
Nov 28, 2020·The Journal of Physical Chemistry. B·Seyedeh Maryam SalehiMarkus Meuwly
Jul 19, 2019·The Journal of Physical Chemistry. B·Jasmine L DesmondMarkus Meuwly

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