Crystal Structures of Spin Labeled T4 Lysozyme Mutants: Implications for the Interpretation of EPR Spectra in Terms of Structure
- 27 June 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (29) , 8396-8405
- https://doi.org/10.1021/bi000604f
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- A Multifrequency Electron Spin Resonance Study of T4 Lysozyme DynamicsBiophysical Journal, 1999
- C—H⋯O hydrogen bond involving proline residues in α-helicesJournal of Molecular Biology, 1998
- Variation in Strength of an Unconventional C−H to O Hydrogen Bond in an Engineered Protein CavityJournal of the American Chemical Society, 1997
- Nonlinear-Least-Squares Analysis of Slow-Motion EPR Spectra in One and Two Dimensions Using a Modified Levenberg–Marquardt AlgorithmJournal of Magnetic Resonance, Series A, 1996
- The Occurence of C–H · · · O Hydrogen Bonds in ProteinsJournal of Molecular Biology, 1995
- Continuous and stopped flow EPR spectrometer based on a loop gap resonatorReview of Scientific Instruments, 1987
- Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolutionJournal of Molecular Biology, 1987
- Stable conformations of aliphatic disulfides: influence of 1,4 interactions involving sulfur atoms.Proceedings of the National Academy of Sciences, 1977
- Shape of the hydrophobic barrier of phospholipid bilayers (Evidence for water penetration in biological membranes)The Journal of Membrane Biology, 1974
- Spin-labelled haemoglobins: A structural interpretation of electron paramagnetic resonance spectra based on X-ray analysisJournal of Molecular Biology, 1971