Carbon-13 nuclear magnetic resonance studies of polyamino acids: The helix-coil transition of poly-l-lysine
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference42 articles.
1. Experimental evidence for the assignment of .alpha.-CH peaks in the nuclear magnetic resonance spectra of polypeptides
2. Helix-coil transition of a synthetic polypeptide monitored by Fourier transform carbon-13 nuclear magnetic resonance
3. The helix–coil transition of poly-(γ-benzylL-glutamate) using13C resonance spectroscopy
4. Carbon-13 Chemical Shifts Accompanying Helix Formation
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1. NMR Studies on Structurally or Dynamically Heterogeneous Systems;Annual Reports on NMR Spectroscopy;2011
2. Characterization of Microbial Poly(ε-l-lysine) and Its Derivatives by Solid-State NMR;ACS Symposium Series;2011-01
3. Effects of hydration on the acid–base interactions and secondary structures of poly-l-lysine probed by 15N and 13C solid state NMR;Physical Chemistry Chemical Physics;2010
4. Acid-Induced Amino Side-Chain Interactions and Secondary Structure of Solid Poly-l-lysine Probed by 15N and 13C Solid State NMR and ab Initio Model Calculations;Journal of the American Chemical Society;2009-05-15
5. Isolation, purification and 13C-and 1H-n.m.r. assignments of peptide [1-24] of human serum albumin;International Journal of Peptide and Protein Research;2009-01-12
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