Isomorphous replacement of cystine with selenocystine in endothelin: oxidative refolding, biological and conformational properties of [Sec3,Sec11,Nle7]-endothelin-1
- 4 December 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 284 (3), 779-792
- https://doi.org/10.1006/jmbi.1998.2189
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Formation of Native Disulfide Bonds in Endothelin-1. Structural Evidence for the Involvement of a Highly Specific Salt Bridge between the Prosequence and the Endothelin-1 SequenceBiochemistry, 1998
- Synthesis of selenocysteine peptides and their oxidation to diselenide-bridged compoundsJournal of Peptide Science, 1997
- Extracting Information from the Temperature Gradients of Polypeptide NH Chemical Shifts. 1. The Importance of Conformational AveragingJournal of the American Chemical Society, 1997
- The Redox Potential of Selenocystine in Unconstrained Cyclic PeptidesAngewandte Chemie International Edition in English, 1997
- [Lys(-2)-Arg(-1)]Endothelin-1 Solution Structure by Two-Dimensional 1H-NMR: Possible Involvement of Electrostatic Interactions in Native Disulfide Bridge Formation and in Biological Activity DecreaseBiochemistry, 1995
- Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysisBiochemistry, 1992
- Determination of the structure of [Nle7]‐endothelin by 1H NMRInternational Journal of Peptide and Protein Research, 1991
- Selenoprotein synthesis: an expansion of the genetic codeTrends in Biochemical Sciences, 1991
- A mild procedure for solid phase peptide synthesis: use of fluorenylmethoxycarbonylamino-acidsJournal of the Chemical Society, Chemical Communications, 1978
- Principles that Govern the Folding of Protein ChainsScience, 1973