Supporting Information A Multifrequency Electron Spin Resonance Study of the Dynamics of Spin Labeled T4 Lysozyme
نویسندگان
چکیده
Ziwei Zhang, Mark R. Fleissner, Dmitriy S. Tipikin, Zhichun Liang, Jozef K. Moscicki, Keith A. Earle, Wayne L. Hubbell, Jack H. Freed 1. Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853 2. Jules Stein Eye Institute and the Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024 3. Smoluchowski Institute of Physics, Jagiellonian University, Reymonta 4, PL-30-059 Krakow, Poland 4. Department of Physics, University of Albany, SUNY, Albany, NY 12222 * Corresponding Author
منابع مشابه
Multifrequency electron spin resonance spectra of a spin-labeled protein calculated from molecular dynamics simulations.
Multifrequency electron spin resonance (ESR) spectra provide a wealth of structural and dynamic information about the local environment of the spin label and, indirectly, about the spin-labeled protein. Relating the features of the observed spectra to the underlying molecular motions and interactions is, however, challenging. To make progress toward a rigorous interpretation of ESR spectra, we ...
متن کاملA multifrequency electron spin resonance study of T4 lysozyme dynamics.
Electron spin resonance (ESR) spectroscopy at 250 GHz and 9 GHz is utilized to study the dynamics and local structural ordering of a nitroxide-labeled enzyme, T4 lysozyme (EC 3.2.1.17), in aqueous solution from 10 degrees C to 35 degrees C. Two separate derivatives, labeled at sites 44 and 69, were analyzed. The 250-GHz ESR spectra are well described by a microscopic ordering with macroscopic d...
متن کاملA Multifrequency Electron Spin Resonance Study of T4 Lysozyme Dynamics Using the Slowly Relaxing Local Structure Model
Electron spin resonance (ESR) spectra were obtained at 250 and 9 GHz for nitroxide-labeled mutants of the protein T4 lysozyme in aqueous solution over a range of temperatures from 2 to 37.5 °C. Two mutants labeled at sites 72 and 131 were studied and compared. The mutant sites are solvent exposed and free of tertiary interactions with other side chains, but the former is at the center of a 5 tu...
متن کاملMultifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.
An extensive set of electron spin resonance spectra was obtained over a wide range of frequencies (9, 95, 170, and 240 GHz) and temperatures (2 to 32 degrees C) to explore the dynamic modes of nitroxide-labeled T4 lysozyme in solution. A commonly used nitroxide side chain (R1), or a methylated analogue with hindered internal motion (R2), was substituted for the native side chain at solvent-expo...
متن کاملStationary-Phase EPR for Exploring Protein Structure, Conformation, and Dynamics in Spin-Labeled Proteins
Proteins tethered to solid supports are of increasing interest in bioanalytical chemistry and protein science in general. However, the extent to which tethering modifies the energy landscape and dynamics of the protein is most often unknown because there are few biophysical methods that can determine secondary and tertiary structures and explore conformational equilibria and dynamics of a tethe...
متن کامل