Design, synthesis and antithrombin activity for conformationally restricted analogs of peptide anticoagulants based on the C-terminal region of the leech peptide, hirudin
- 1 November 1988
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 957 (1) , 53-59
- https://doi.org/10.1016/0167-4838(88)90156-2
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- N-Terminal requirements of small peptide anticoagulants based on hirudin 54-65Journal of Medicinal Chemistry, 1988
- Anticoagulant peptides. Nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombinJournal of Medicinal Chemistry, 1987
- The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamicsThe EMBO Journal, 1987
- Antithrombin properties of C‐terminus of hirudin using synthetic unsulfated Nα‐acetyl‐hirudin45–65FEBS Letters, 1987
- Proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structureBiochemistry, 1987
- The hydrophobic moment detects periodicity in protein hydrophobicity.Proceedings of the National Academy of Sciences, 1984