Solvent accessibility in folded proteins. Studies of hydrogen exchange in trypsin
Open Access
- 4 January 1975
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (2) , 432-439
- https://doi.org/10.1016/s0021-9258(19)41917-0
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- The interpretation of protein structures: Estimation of static accessibilityPublished by Elsevier ,2004
- Environment and exposure to solvent of protein atoms. Lysozyme and insulinPublished by Elsevier ,2004
- The interpretation of protein structures: Total volume, group volume distributions and packing densityPublished by Elsevier ,2004
- Structure of α-lactalbumin and its fluctuationJournal of Molecular Biology, 1973
- Effects of ligand binding on the rates of hydrogen exchange in myoglobin and hemoglobinBiochemistry, 1973
- Fluctuation of the lysozyme structure: II. Effects of temperature and binding of inhibitorsJournal of Molecular Biology, 1973
- Ligand binding and internal equilibiums in proteinsBiochemistry, 1972
- Thermodynamics of transfer of amides from an apolar to an aqueous solutionBiochemistry, 1969
- Trypsinogen, Trypsin, Trypsin-Substrate and Trypsin-Inhibitor Complexes in Urea SolutionsEuropean Journal of Biochemistry, 1968
- Slow hydrogen-deuterium exchange in a non-.alpha.-helical polyamideJournal of the American Chemical Society, 1967