Reduced-denatured ribonuclease A is not in a compact state
- 12 February 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 380 (1-2) , 179-182
- https://doi.org/10.1016/0014-5793(96)00048-8
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Application of dynamic light scattering to studies of protein folding kineticsEuropean Biophysics Journal, 1992
- Denatured states of ribonuclease A have compact dimensions and residual secondary structureBiochemistry, 1992
- Analysis of hydrodynamic data for denatured globular proteins in terms of the wormlike cylinder modelInternational Journal of Biological Macromolecules, 1991
- Conformational unfolding in the N‐terminal region of ribonuclease a detected by nonradiative energy transfer: Distribution of interresidue distances in the native, denatured, and reduced‐denatured statesBiopolymers, 1988
- Local secondary structure in ribonuclease A denatured by guanidine · HCl near 1 °CJournal of Molecular Biology, 1982
- A constrained regularization method for inverting data represented by linear algebraic or integral equationsComputer Physics Communications, 1982
- Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and b-LactoglobulinJournal of Biological Chemistry, 1974
- Statistical mechanics of chain moleculesBiopolymers, 1969
- Dimensions of protein random coilsBiochemistry, 1968
- Proteins in 6 m Guanidine HydrochlorideJournal of Biological Chemistry, 1966