Secondary structure formation and stability
- 1 February 1992
- journal article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 2 (1) , 13-20
- https://doi.org/10.1016/0959-440x(92)90170-c
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- How does protein synthesis give rise to the 3D‐structure?FEBS Letters, 1991
- Mutational analysis of protein stability: Current Opinion in Structural Biology 1991, 1:17–21Current Opinion in Structural Biology, 1991
- An early immunoreactive folding intermediate of the tryptophan synthase β2 subunit is a ‘molten globule’FEBS Letters, 1990
- Helix‐coil stability constants for the naturally occurring amino acids in water. XXIII. Proline parameters from random poly(hydroxybutylglutamine‐CO‐L‐proline)Biopolymers, 1990
- Helix‐coil stability constants for the naturally occurring amino acids in water. XXIV. Half‐cystine parameters from random poly(hydroxybutylglutamine‐CO‐S‐methylthio‐L‐cysteine)Biopolymers, 1990
- MUTATIONAL EFFECTS ON PROTEIN STABILITYAnnual Review of Biochemistry, 1989
- Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectraBiochemistry, 1988
- An early intermediate of refolding α‐lactalbumin forms within 20 msFEBS Letters, 1987
- Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroismFEBS Letters, 1987
- Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. II. Characterization of the Host Polymers and Application of the Host-Guest Technique to Random Poly(hydroxypropylglutamine-co-hydroxybutylglutamine)Macromolecules, 1971