MEARA Sequence Repeat of Human CstF-64 Polyadenylation Factor Is Helical in Solution. A Spectroscopic and Calorimetric Study
- 1 September 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 38 (39) , 12869-12875
- https://doi.org/10.1021/bi990724r
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- [2] Modified amino acids as probes of helix stabilityPublished by Elsevier ,1998
- Local Interactions in Protein Folding: Lessons from the α-HelixJournal of Biological Chemistry, 1997
- The α-Helix of Ribonuclease T1as an Independent Stability Unit: Direct Comparison of Peptide and Protein StabilityJournal of Molecular Biology, 1996
- High Helical Propensity of the Peptide Fragments Derived from β-Lactoglobulin, a Predominantly β-sheet ProteinJournal of Molecular Biology, 1995
- α‐Helix‐forming propensities in peptides and proteinsProteins-Structure Function and Bioinformatics, 1994
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- The Mechanism of alpha-Helix Formation by PeptidesAnnual Review of Biophysics, 1992
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Thermodynamic Characterization of Conformational States of Biological Macromolecules using Differential Scanning CalorimetryCRC Critical Reviews in Biochemistry, 1978