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Biochemistry|January 30, 1990
Positional independence and additivity of amino acid replacements on helix stability in monomeric peptidesG Merutka, E StellwagenBiochemistry|February 12, 1991
Effect of amino acid ion pairs on peptide helicityG Merutka, E StellwagenBiochemistry|April 30, 1991
A model peptide with enhanced helicityG Merutka, W Shalongo, E StellwagenJournal of Biomolecular NMR|January 1, 1995
'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGGG Merutka, H J Dyson, P E WrightBiochemistry|December 7, 1993
NMR evidence for multiple conformations in a highly helical model peptideG Merutka, D Morikis, R Brüschweiler, et al.Biochemistry|August 14, 1990
Effect of central-residue replacements on the helical stability of a monomeric peptideG Merutka, W Lipton, W Shalongo, et al.Protein Science : a Publication of the Protein Society|March 1, 1997
Folding propensities of peptide fragments of myoglobinM T Reymond, G Merutka, H J Dyson, et al.Journal of Molecular Biology|August 5, 1992
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. MyohemerythrinH J Dyson, G Merutka, J P Waltho, et al.Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobinJ P Waltho, V A Feher, G Merutka, et al.Pageof 2