The homologous angiogenin and ribonuclease N-terminal fragments fold into very similar helices when isolated
- 14 February 1992
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 182 (3) , 1491-1498
- https://doi.org/10.1016/0006-291x(92)91902-3
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Secondary‐structure dependent chemical shifts in proteinsBiopolymers, 1990
- Characterization of low populated peptide helical structures in solution by means of NMR proton conformational shiftsBiochemical and Biophysical Research Communications, 1990
- Conformational properties of the isolated 1–23 fragment of human hemoglobin α-chainBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Location of an .alpha.-helix in fragment 96-133 from bovine somatotropin by proton NMR spectroscopyBiochemistry, 1988
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Determinants of a protein foldJournal of Molecular Biology, 1987
- NH resonances of Ribonuclease S‐peptide in aqueous solution. Low temperature n.m.r. studyInternational Journal of Peptide and Protein Research, 1985
- On the fundamental role of the glu 2−…Arg 10+ salt bridge in the folding of isolated ribonuclease a S-peptideBiochemical and Biophysical Research Communications, 1984
- Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptideFEBS Letters, 1983
- 1H n.m.r. parameters of the N‐terminal 19‐residue S‐peptide of ribonuclease in aqueous solutionInternational Journal of Peptide and Protein Research, 1983