Author(s) : Teilum, K. , Hoch, J. C. , Goffin, Vincent , Kinet, Sandrina , Martial, Joseph , Kragelund, B. B.

Description : We report the solution structure of human prolactin determined by NMR spectroscopy. Our result is a significant improvement over a previous structure in terms of number and distribution of distance restraints, regularity of secondary structure, and potential energy. More significantly, the structure...

Repository : ORBi (University of Liège) , View repository documents

Language(s) : English

Subject(s) : Amino Acid Sequence , Animals , Binding Sites , Human Growth Hormone/chemistry/genetics/metabolism , Humans , Models, Molecular , Molecular Sequence Data , Nuclear Magnetic Resonance, Biomolecular , Placental Lactogen/chemistry/genetics , Prolactin/*chemistry/genetics/metabolism , Protein Conformation , Receptors, Prolactin/genetics/metabolism , Recombinant Proteins/chemistry/genetics/metabolism , Sequence Homology, Amino Acid , Sheep , Solutions , Life sciences :: Biochemistry, biophysics & molecular biology [F05] , Sciences du vivant :: Biochimie, biophysique & biologie moléculaire [F05]

Publisher(s) :

Contributor(s) : Giga-Development and Stem Cells

Source(s) : &ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&jtitle=Journal+of+Molecular+Biology&issn=0022-2836&eissn=1089-8638&volume=351&issue=4&pages=810-23&pub=Academic+Press&place=London&place=United+Kingdom

Publication Date(s) : 2005-01-01