Hydroiodic acid attachment kinetics as a chemical probe of gaseous protein ion structure: Bovine pancreatic trypsin inhibitor
- 1 June 1999
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Society for Mass Spectrometry
- Vol. 10 (6) , 552-556
- https://doi.org/10.1016/s1044-0305(99)00026-4
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Simulations of the structural and dynamical properties of denatured proteins: the “molten coil” state of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1998
- High resolution ion mobility measurements for gas phase proteins: correlation between solution phase and gas phase conformationsInternational Journal of Mass Spectrometry and Ion Processes, 1997
- Protein Unfolding Pathways Explored Through Molecular Dynamics SimulationsJournal of Molecular Biology, 1993
- Probing qualitative conformation differences of multiply protonated gas-phase proteins via hydrogen/deuterium isotopic exchange with water-d2Journal of the American Chemical Society, 1992
- Proton affinity of arginine measured by the kinetic approachRapid Communications in Mass Spectrometry, 1992
- Proton affinities of the 20 common .alpha.-amino acidsJournal of the American Chemical Society, 1992
- Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltonsAnalytical Chemistry, 1988
- Structure of form III crystals of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1987
- Protein dynamics in solution and in a crystalline environment: a molecular dynamics studyBiochemistry, 1982
- Protein structural fluctuations during a period of 100 psNature, 1979