Protein Fluctuations and Cavity Changes Relationship

2018 ◽  
Vol 14 (2) ◽  
pp. 998-1008 ◽  
Author(s):  
German P. Barletta ◽  
Sebastian Fernandez-Alberti
Keyword(s):  
2018 ◽  
Author(s):  
Cerys S Manning ◽  
Veronica Biga ◽  
James Boyd ◽  
Jochen Kursawe ◽  
Bodvar Ymisson ◽  
...  

AbstractDuring embryogenesis cells make fate decisions within complex tissue environments. The levels and dynamics of transcription factor expression regulate these decisions. Here we use single cell live imaging of an endogenous HES5 reporter and absolute protein quantification to gain a dynamic view of neurogenesis in the embryonic mammalian spinal cord. We report that dividing neural progenitors show both aperiodic and periodic HES5 protein fluctuations. Mathematical modelling suggests that in progenitor cells the HES5 oscillator operates close to its bifurcation boundary where stochastic conversions between dynamics are possible. HES5 expression becomes more frequently periodic as cells transition to differentiation which, coupled with an overall decline in HES5 expression, creates a transient period of oscillations with higher fold expression change. This increases the decoding capacity of HES5 oscillations and correlates with interneuron versus motor neuron cell fate. Thus, HES5 undergoes complex changes in gene expression dynamics as cells differentiate.


2016 ◽  
Vol 110 (3) ◽  
pp. 228a-229a
Author(s):  
Suchithranga M.D.C. Perera ◽  
Utsab Shrestha ◽  
Debsindhu Bhowmik ◽  
Udeep Chawla ◽  
Andrey V. Struts ◽  
...  

2018 ◽  
Vol 20 (6) ◽  
pp. 4360-4372 ◽  
Author(s):  
Pavel Malý ◽  
Alastair T. Gardiner ◽  
Richard J. Cogdell ◽  
Rienk van Grondelle ◽  
Tomáš Mančal

Ultrafast bulk and single-molecule spectroscopy experiments described by a single theoretical model show how protein fluctuations influence photosynthetic light harvesting.


2020 ◽  
Vol 117 (39) ◽  
pp. 24061-24068 ◽  
Author(s):  
Thomas T. Foley ◽  
Katherine M. Kidder ◽  
M. Scott Shell ◽  
W. G. Noid

The success of any physical model critically depends upon adopting an appropriate representation for the phenomenon of interest. Unfortunately, it remains generally challenging to identify the essential degrees of freedom or, equivalently, the proper order parameters for describing complex phenomena. Here we develop a statistical physics framework for exploring and quantitatively characterizing the space of order parameters for representing physical systems. Specifically, we examine the space of low-resolution representations that correspond to particle-based coarse-grained (CG) models for a simple microscopic model of protein fluctuations. We employ Monte Carlo (MC) methods to sample this space and determine the density of states for CG representations as a function of their ability to preserve the configurational information, I, and large-scale fluctuations, Q, of the microscopic model. These two metrics are uncorrelated in high-resolution representations but become anticorrelated at lower resolutions. Moreover, our MC simulations suggest an emergent length scale for coarse-graining proteins, as well as a qualitative distinction between good and bad representations of proteins. Finally, we relate our work to recent approaches for clustering graphs and detecting communities in networks.


1999 ◽  
Vol 19 (1-4) ◽  
pp. 19-34 ◽  
Author(s):  
K. D. Rector ◽  
M. D. Fayer

Ps infrared vibrational echo experiments on myoglobin and myoglobin mutants are presented. The vibrational dephasing experiments examine the influence of protein dynamics on the CO ligand, at the active site of myoglobin, from low temperature to physiologically relevant temperatures. The vibrational echo results are combined with measurements of the CO vibrational lifetime to yield the homogeneous pure dephasing. The pure dephasing is the Fourier transform of the homogeneous linewidth with the lifetime contribution removed. The mutant H64V protein's CO vibrational pure dephasing rate is ∼20% slower (narrower pure dephasing linewidth) than the native protein at all temperatures, although the only difference between the two proteins is the replacement of the native’s polar distal histidine by a non-polar valine. The mutant H93G(N-MeIm) pure dephasing is identical to the native's, despite the severing of the only covalent bond between the heme and the globin. These results provide insights into the mechanisms of the transmission of protein fluctuations to the CO ligand bound at the active site.


2010 ◽  
Vol 132 (16) ◽  
pp. 5693-5703 ◽  
Author(s):  
Víctor A. Lórenz-Fonfría ◽  
Yuji Furutani ◽  
Toru Ota ◽  
Kazutomo Ido ◽  
Hideki Kandori

Biochemistry ◽  
2005 ◽  
Vol 44 (13) ◽  
pp. 5095-5105 ◽  
Author(s):  
Karin Nienhaus ◽  
Andreas Ostermann ◽  
G. Ulrich Nienhaus ◽  
Fritz G. Parak ◽  
Marius Schmidt

Sign in / Sign up

Export Citation Format

Share Document