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Biopolymers|January 1, 1993
Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 2. Comparison of spectral and chromatographic kinetic analysesW Shalongo, M Jagannadham, E StellwagenBiochemistry|July 13, 1993
Residue helix parameters obtained from dichroic analysis of peptides of defined sequenceS H Park, W Shalongo, E StellwagenProteins|October 21, 1998
Analysis of N-terminal capping using carbonyl-carbon chemical shift measurementsS H Park, W Shalongo, E StellwagenBiochemistry|November 30, 1993
Modulation of the helical stability of a model peptide by ionic residuesS H Park, W Shalongo, E StellwagenProtein Science : a Publication of the Protein Society|August 1, 1997
The role of PII conformations in the calculation of peptide fractional helix contentS H Park, W Shalongo, E StellwagenBiochemistry|June 2, 1987
Refolding of denatured thioredoxin observed by size-exclusion chromatographyW Shalongo, R Ledger, M V Jagannadham, et al.Biochemistry|May 30, 1989
Refolding of denatured ribonuclease observed by size exclusion chromatographyW Shalongo, M V Jagannadham, C Flynn, et al.Biochemistry|March 10, 1987
Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxinR F Kelley, W Shalongo, M V Jagannadham, et al.Biopolymers|September 1, 1992
The contribution of residue ion pairs to the helical stability of a model peptideE Stellwagen, S H Park, W Shalongo, et al.Biochemistry|November 24, 1992
A kinetic study of the folding of staphylococcal nuclease using size-exclusion chromatographyW Shalongo, M V Jagannadham, P Heid, et al.Pageof 8