BMC Biophys 2014 16;7. Epub 2014 Aug 16.
Physics Department, Carnegie Mellon University, Pittsburgh 15213, PA, USA.
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J Biol Phys 2014 Mar 30;40(2):121-37. Epub 2014 Mar 30.
Physics Department, Carnegie Mellon University, 15213, Pittsburgh, PA, USA,
Predicting the conformational changes in proteins that are relevant for substrate binding is an ongoing challenge in the aim of elucidating the functional states of proteins. The motions that are induced by protein-ligand interactions are governed by the protein global modes. Our measurements indicate that the detected changes in the global backbone motion of the enzyme upon binding reflect a shift from the large-scale collective dominant mode in the unbound state towards a functional twisting deformation that assists in closing the binding cleft. Read More
Phys Rev E Stat Nonlin Soft Matter Phys 2010 Mar 23;81(3 Pt 1):031915. Epub 2010 Mar 23.
Physics Department, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
THz spectroscopy is used to investigate the dynamics of the globular protein hen egg white lysozyme under varying hydration and temperature conditions. An analysis of the experimental spectra has revealed that the amount of solvent in the hydration shell has a strong influence on the low-frequency protein conformational dynamics and also the arrangement of hydrogen bonds in the protein secondary structure. Furthermore at a hydration level >0. Read More
Phys Chem Chem Phys 2012 May 2;14(18):6375-81. Epub 2012 Apr 2.
IFW Dresden, Leibniz Institute for Solid State and Materials Research, D-01171 Dresden, Germany.
We investigate the nature of the solvent motions giving rise to the rapid temperature dependence of protein picoseconds motions at 220 K, often referred to as the protein dynamical transition. The interdependence of picoseconds dynamics on hydration and temperature is examined using terahertz time domain spectroscopy to measure the complex permittivity in the 0.2-2. Read More
Biophys J 2011 Aug;101(4):925-33
Department of Physical Chemistry II, Ruhr-University Bochum, Bochum, Germany.
We investigate the thermal denaturation of human serum albumin and the associated solvation using terahertz (THz) spectroscopy in aqueous buffer solution. Far- and near-ultraviolet circular dichroism spectroscopy reveal that the protein undergoes a native (N) to extended (E) state transition at temperature ≤55°C with a marginal change in the secondary and tertiary structure. At 70°C, the protein transforms into an unfolded (U) state with significant irreversible disruption of its structures. Read More