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FEBS Letters|November 28, 1994
Does the solid-state structure of endothelin-1 provide insights concerning the solution-state conformational equilibrium?G M Lee, C Chen, T M Marschner, et al.FEBS Letters|April 9, 1991
Conformation of endothelin in aqueous ethylene glycol determined by 1H-NMR and molecular dynamics simulationsS R Krystek, D A Bassolino, J Novotny, et al.Basic Life Sciences|January 1, 1990
Computer-aided conformational analysis based on NOESY signal intensitiesN H Andersen, X N Lai, P K Hammen, et al.Biochemistry|February 21, 1992
Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysisN H Andersen, C P Chen, T M Marschner, et al.Biochemical and Biophysical Research Communications|April 30, 1992
Peptide/protein structure analysis using the chemical shift index method: upfield alpha-CH values reveal dynamic helices and alpha L sitesN H Andersen, B Cao, C ChenProtein Science : a Publication of the Protein Society|September 23, 1997
Empirical parameterization of a model for predicting peptide helix/coil equilibrium populationsN H Andersen, H TongBiochemistry|June 16, 1987
Pyridine coenzyme analogues. Synthesis and characterization of alpha- and beta-nicotinamide arabinoside adenine dinucleotidesB L Kam, O Malver, T M Marschner, et al.Biochemical and Biophysical Research Communications|April 30, 1984
High-field 1H NMR studies of prostaglandin H2 and its decomposition pathwaysN H Andersen, C J HartzellBiochemistry|April 23, 1985
500-MHz proton NMR studies of the medium-dependent conformational preference of prostaglandin F2 alpha analoguesN H Andersen, B S LinProstaglandins|November 1, 1975
Molecular basis of prostaglandin potency. II. Proton NMR studies of the conformation of prostaglandin F2alphaE M Leovey, N H AndersenPageof 1,209