An approach to the three-dimensional structure of bovine growth hormone based on chemical modification and secondary structure prediction.
Three different methods have been applied to the prediction of secondary structure. The prediction that better fitted the chemical data was chosen. Two regions of the bovine growth hormone molecule (111-117 and 166-174) appear to be exposed to the solvent, according to hydropathic analysis but have several charged residues not reactive towards their specific reagents. Two molecular domains are postulated, each one bearing a region with charged residues on its surface and interacting with the other in the molecule by means of saline bridges. The hydrophobic core of the molecule is formed by the ensemble of the hydrophobic region predicted between residues 81 and 108, and the hydrophobic faces of the amphiphilic helices 109-127 and 9-33.
Ermacora
M
M
Instituto de Química y Físico-química Biológicas (UBA-CONICET) Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina.
Cascone
O
O
Wolfenstein-Todel
C
C
Biscoglio de Jimenez Bonino
M
M
Nowicki
C
C
Rivero
J L
JL
Santome
J A
JA
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D013006:Growth Hormone / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014961:X-Ray Diffraction
D013006:Growth Hormone