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Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana
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Letter to the editor: Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe
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Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate
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p13SUC1 and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope
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Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein
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The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase
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Recombinant production of the p10CKS1At protein from Arabidopsis thaliana and 13C and 15N double-isotopic enrichment for NMR studies
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TRANSFER NUCLEAR OVERHAUSER EFFECT STUDY OF THE CONFORMATION OF OXYTOCIN BOUND TO BOVINE NEUROPHYSIN-I.
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T-1 RELAXATION-TIME OF WATER FROM A MOLECULAR-DYNAMICS SIMULATION.
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Transfer NOE study of oxytocin bound to neurophysin
(1992)