Conformational transitions in poly(l-lysine): studies using Fourier transform infrared spectroscopy
- 1 September 1989
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 998 (1) , 75-79
- https://doi.org/10.1016/0167-4838(89)90121-0
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- [13] Resolution-enhanced fourier transform infrared spectroscopy of enzymesPublished by Elsevier ,1986
- Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and ProteinsAdvances in Protein Chemistry, 1986
- Vibrational circular dichroism of polypeptides, V. A study of 310‐helical‐octapeptidesBiopolymers, 1986
- The solution conformation of poly(L‐lysine). A Raman and infrared spectroscopic studyBiopolymers, 1976
- Circular dichroism and proton magnetic resonance studies of random chain poly-L-lysineBiopolymers, 1974
- Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random formsBiopolymers, 1973
- Circular dichroism of the “random” polypeptide chainBiopolymers, 1969
- Infrared Spectra and Protein Conformations in Aqueous SolutionsJournal of Biological Chemistry, 1967
- INFRARED SPECTRA AND PROTEIN CONFORMATIONS IN AQUEOUS SOLUTIONS .I. AMIDE I BAND IN H2O AND D2O SOLUTIONS1967
- The circular dichroism of the β structure of poly-l-lysineBiochemical and Biophysical Research Communications, 1966