Coupling of protein relaxation to ligand binding and migration in myoglobin

Biophysical Journal
N Agmon

Abstract

Protein relaxation, ligand binding, and ligand migration into a hydrophobic cavity in myoglobin are unified by a bounded diffusion model which produces an accurate fit to complex ligand rebinding data over eight decades in time and a 160 K temperature range, in qualitative agreement with time-resolved x-ray crystallography. Protein relaxation operates in a cyclic manner to move the ligand away from the binding site.

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Citations

Oct 30, 2009·International Journal of Molecular Sciences·Vangelis Daskalakis, Constantinos Varotsis
May 9, 2012·The Journal of Chemical Physics·Takayuki TsudukiTakahisa Yamato
Nov 8, 2013·The Journal of Physical Chemistry. B·Shuji Kaieda, Bertil Halle
May 12, 2005·Biochimica Et Biophysica Acta·Lorenzo CordoneCristiano Viappiani
Dec 6, 2005·Biophysical Journal·David R Nutt, Markus Meuwly
Aug 6, 2009·Journal of the American Chemical Society·Mariano Andrea ScorciapinoMatteo Ceccarelli
May 2, 2013·Journal of the American Chemical Society·Mariano Andrea ScorciapinoMatteo Ceccarelli
Dec 1, 2006·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Stefania AbbruzzettiCristiano Viappiani
Dec 27, 2019·Biophysical Chemistry·Kirthi Joshi, Abani K Bhuyan
Jul 21, 2006·The Journal of Physical Chemistry. B·Silvia SottiniAndrea Mozzarelli
Jul 21, 2006·The Journal of Physical Chemistry. B·Polina Banushkina, Markus Meuwly
Mar 3, 2006·The Journal of Physical Chemistry. B·Rinat GepshteinNoam Agmon
Dec 8, 2005·Journal of the American Chemical Society·Silvia SottiniCristiano Viappiani
Jul 21, 2006·The Journal of Physical Chemistry. B·Silvia SottiniAndrea Mozzarelli

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