Lysine side-chain dynamics derived from 13C-multiplet NMR relaxation studies on di- and tripeptides
- 1 June 1995
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 5 (4) , 397-410
- https://doi.org/10.1007/bf00182283
Abstract
No abstract availableKeywords
This publication has 6 references indexed in Scilit:
- Tri- and diglycine backbone rotational dynamics investigated by carbon-13 NMR multiplet relaxation and molecular dynamics simulationsBiochemistry, 1993
- Dynamics of methyl groups in proteins as studied by proton-detected carbon-13 NMR spectroscopy. Application to the leucine residues of staphylococcal nucleaseBiochemistry, 1992
- Large-amplitude nonlinear motions in proteinsPhysical Review Letters, 1992
- Fluorescence, CD, attenuated total reflectance (ATR) FTIR, and carbon-13 NMR characterization of the structure and dynamics of synthetic melittin and melittin analogs in lipid environmentsBiochemistry, 1992
- Fluorescence and carbon-13 NMR determination of side-chain and backbone dynamics of synthetic melittin and melittin analogs in isotropic solventsBiochemistry, 1989
- Dynamics of folded proteinsNature, 1977