Conformational properties of the isolated 1–23 fragment of human hemoglobin α-chain
- 1 December 1988
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 957 (3) , 380-389
- https://doi.org/10.1016/0167-4838(88)90229-4
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Determination of local conformational stability in fragment 96-133 of bovine growth hormone by high-resolution proton NMR spectroscopyBiochemistry, 1988
- A two‐dimensional NMR study of the antimicrobial peptide magainin 2FEBS Letters, 1988
- 1H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragmentFEBS Letters, 1987
- Permissible discontinuity region of the .alpha.-chain of hemoglobin: noncovalent interaction of heme and the complementary fragments .alpha.1-30 and .alpha.31-141Biochemistry, 1986
- Allosteric sensitivity in hemoglobin at the .alpha.-subunit N-terminus studied by hydrogen exchangeBiochemistry, 1986
- Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coliJournal of Molecular Biology, 1985
- NH resonances of Ribonuclease S‐peptide in aqueous solution. Low temperature n.m.r. studyInternational Journal of Peptide and Protein Research, 1985
- Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptideFEBS Letters, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- 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