Low frequency vibrations of amino acid homopolymers observed by synchrotron far-ir absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra
- 7 May 1999
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 49 (7) , 591-603
- https://doi.org/10.1002/(sici)1097-0282(199906)49:7<591::aid-bip5>3.0.co;2-q
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Effect of Solvent on Collective Motions in Globular ProteinJournal of Molecular Biology, 1993
- Internal water molecules and H‐bonding in biological macromolecules: A review of structural features with functional implicationsProtein Science, 1992
- The iron-histidine mode of myoglobin revisited: resonance Raman studies of isotopically labeled Escherichia coli-expressed myoglobinJournal of the American Chemical Society, 1991
- Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulationsProteins-Structure Function and Bioinformatics, 1991
- Low-Frequency Parametrization of Hydrogen BondingJournal of Biomolecular Structure and Dynamics, 1991
- Far-infrared perturbation of reaction rates in myoglobin at low temperaturesPhysical Review Letters, 1989
- Low-frequency collective motion in biomacromolecules and its biological functionsBiophysical Chemistry, 1988
- Origin of low-frequency motions in biological macromolecules: A view of recent progress in the quasi-continuity modelBiophysical Chemistry, 1986
- [16] Resonance Raman studies of ligand bindingPublished by Elsevier ,1986
- [18] Low frequency vibrations and the dynamics of proteins and polypeptidesPublished by Elsevier ,1979