Temperature Dependence

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David Baker - One of the best experts on this subject based on the ideXlab platform.

  • Protein folding kinetics exhibit an Arrhenius Temperature Dependence when corrected for the Temperature Dependence of protein stability
    Proceedings of the National Academy of Sciences of the United States of America, 1997
    Co-Authors: Michelle L. Scalley, David Baker
    Abstract:

    The anomalous Temperature Dependence of protein folding has received considerable attention. Here we show that the Temperature Dependence of the folding of protein L becomes extremely simple when the effects of Temperature on protein stability are corrected for; the logarithm of the folding rate is a linear function of 1/T on constant stability contours in the Temperature–denaturant plane. This convincingly demonstrates that the anomalous Temperature Dependence of folding derives from the Temperature Dependence of the interactions that stabilize proteins, rather than from the super Arrhenius Temperature Dependence predicted for the configurational diffusion constant on a rough energy landscape. However, because of the limited Temperature range accessible to experiment, the results do not rule out models with higher order Temperature Dependences. The significance of the slope of the stability-corrected Arrhenius plots is discussed.

Dmitry Budker - One of the best experts on this subject based on the ideXlab platform.

  • Temperature Dependence of the nitrogen vacancy magnetic resonance in diamond
    Physical Review Letters, 2010
    Co-Authors: Victor M Acosta, Erik Bauch, M P Ledbetter, A Waxman, Louiss Bouchard, Dmitry Budker
    Abstract:

    The Temperature Dependence of the magnetic-resonance spectra of nitrogen-vacancy (${\mathrm{NV}}^{\ensuremath{-}}$) ensembles in the range of 280--330 K was studied. Four samples prepared under different conditions were analyzed with ${\mathrm{NV}}^{\ensuremath{-}}$ concentrations ranging from 10 ppb to 15 ppm. For all samples, the axial zero-field splitting (ZFS) parameter $D$ was found to vary significantly with Temperature, $T$, as $dD/dT=\ensuremath{-}74.2(7)\text{ }\text{ }\mathrm{kHz}/\mathrm{K}$. The transverse ZFS parameter $E$ was nonzero (between 4 and 11 MHz) in all samples, and exhibited a Temperature Dependence of $dE/(EdT)=\ensuremath{-}1.4(3)\ifmmode\times\else\texttimes\fi{}{10}^{\ensuremath{-}4}\text{ }\text{ }{\mathrm{K}}^{\ensuremath{-}1}$. The results might be accounted for by considering local thermal expansion. The Temperature Dependence of the ZFS parameters presents a significant challenge for diamond magnetometers and may ultimately limit their bandwidth and sensitivity.

A. Joshua Wand - One of the best experts on this subject based on the ideXlab platform.

  • Temperature Dependence of Fast Dynamics in Proteins
    Biophysical journal, 2007
    Co-Authors: Xiang-jin Song, Peter F. Flynn, Kim A. Sharp, A. Joshua Wand
    Abstract:

    The Temperature Dependence of the internal dynamics of recombinant human ubiquitin has been measured using solution NMR relaxation techniques. Nitrogen-15 relaxation has been employed to obtain a measure of the amplitude of sub- nanosecond motion at amide N-H sites in the protein. Deuterium relaxation has been used to obtain a measure of the amplitude of motion of methyl-groups in amino-acid side chains. Data was obtained between 5 and 55� C. The majority of amide N-H and methyl groups show a roughly linear (R 2 . 0.75) Temperature Dependence of the associated Lipari-Szabo model-free squared generalized-order parameter (O 2 ) describing the amplitude of motion. Interestingly, for those sites showing a linear response, the Temperature Dependence of the backbone is distinct from that of the methyl-bearing side chains with the former being char- acterized by a significantly larger L-value, where L is defined as d ln(1 � O)/d lnT. These results are comparable to the sole previous such study of the Temperature Dependence of protein motion obtained for a calmodulin-peptide complex. This suggests that the distinction between the main chain and methyl-bearing side chains may be general. Insight into the Temperature depen- dence is gathered from a simple two-state step potential model.

A. Sardesai - One of the best experts on this subject based on the ideXlab platform.

  • Anomalous Temperature Dependence of photoluminescence in porous silicon
    Applied Physics Letters, 1993
    Co-Authors: K. L. Narasimhan, Sangam Banerjee, Awadhesh Kumar Srivastava, A. Sardesai
    Abstract:

    We have studied the Temperature Dependence of luminescence in porous silicon between 10 and 300 K. We find that above 60 K the luminescence has a Temperature Dependence opposite in sign from that of the band gap. Using a Gaussian decomposition procedure we have identified three different processes which dominate the luminescence at different Temperatures. With a knowledge of the Temperature Dependence of the relative intensities of the three components we explain the blue shift of the luminescence peak with increasing Temperature. We also present arguments to show that the luminescence in porous silicon is due to a complex.

Michelle L. Scalley - One of the best experts on this subject based on the ideXlab platform.

  • Protein folding kinetics exhibit an Arrhenius Temperature Dependence when corrected for the Temperature Dependence of protein stability
    Proceedings of the National Academy of Sciences of the United States of America, 1997
    Co-Authors: Michelle L. Scalley, David Baker
    Abstract:

    The anomalous Temperature Dependence of protein folding has received considerable attention. Here we show that the Temperature Dependence of the folding of protein L becomes extremely simple when the effects of Temperature on protein stability are corrected for; the logarithm of the folding rate is a linear function of 1/T on constant stability contours in the Temperature–denaturant plane. This convincingly demonstrates that the anomalous Temperature Dependence of folding derives from the Temperature Dependence of the interactions that stabilize proteins, rather than from the super Arrhenius Temperature Dependence predicted for the configurational diffusion constant on a rough energy landscape. However, because of the limited Temperature range accessible to experiment, the results do not rule out models with higher order Temperature Dependences. The significance of the slope of the stability-corrected Arrhenius plots is discussed.