Secondary structure changes stabilize the reactive-centre cleaved form of SERPINs: A study by 1H nuclear magnetic resonance and Fourier transform infrared spectroscopy
- 20 December 1992
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 228 (4) , 1235-1254
- https://doi.org/10.1016/0022-2836(92)90329-i
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Mobile reactive centre of serpins and the control of thrombosisNature, 1991
- Crystal structure of cleaved human α1-antichymotrypsin at 2.7 å resolution and its comparison with other serpinsJournal of Molecular Biology, 1991
- Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methodsBiochemistry, 1990
- Crystal structure of bovine antithrombin IIIActa crystallographica Section B, Structural science, crystal engineering and materials, 1990
- Protein secondary structures in water from second-derivative amide I infrared spectraBiochemistry, 1990
- C1 Inhibitor and Hereditary Angioneurotic EdemaAnnual Review of Immunology, 1988
- Examination of the secondary structure of proteins by deconvolved FTIR spectraBiopolymers, 1986
- Plakalbumin, α1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosisNature, 1985
- α1-Antitrypsin and the serpins: variation and countervariationTrends in Biochemical Sciences, 1985
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979