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Indian J Biochem Biophys ; 1992 Jun; 29(3): 231-5
Article in English | IMSEAR | ID: sea-26868

ABSTRACT

Various two-dimensional NMR techniques have been used to obtain complete resonance assignments of the protons in the 1-10 fragment of adrenocorticotropic hormone (ACTH). 1H-1H coupling constants among the backbone protons and the chemical shift values measured in aqueous and in dimethyl sulphoxide solutions indicated preference for extended but different conformations in the two solvents.


Subject(s)
Adrenocorticotropic Hormone/chemistry , Amino Acid Sequence , Magnetic Resonance Spectroscopy/methods , Molecular Sequence Data , Peptide Fragments/chemistry , Protein Conformation , Solvents
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