Pressure-induced reversible changes in secondary structure of poly(L-lysine): An ir spectroscopic study
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference22 articles.
1. Folding of the nascent peptide chain into a biologically active protein
2. (1986) in High Pressure Chemistry and Biochemistry, & Eds., Reidel, D., Publishing Company, Boston, pp. 401-420.
3. Pressure effects on the Raman spectra of proteins: Pressure-induced changes in the conformation of lysozyme in aqueous solutions
4. Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopic study
5. Crystalline Quartz as an Internal Pressure Calibrant for High-Pressure Infrared Spectroscopy
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3. Effects of Cosolvents and Macromolecular Crowding on the Phase Transitions and Temperature-Pressure Stability of Chiral and Racemic Poly-Lysine;Zeitschrift für Physikalische Chemie;2018-01-08
4. Application of MCR-ALS to reveal intermediate conformations in the thermally induced α-β transition of poly- l -lysine monitored by FT-IR spectroscopy;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2017-10
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