A theoretical study of the structure of parathyroid hormone.
- 1 July 1980
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 77 (7) , 3791-3795
- https://doi.org/10.1073/pnas.77.7.3791
Abstract
Theoretical analysis of the tertiary and secondary structure of parathyroid hormone was conducted. By combining interpretations from this analysis with chemical data available in the literature, certain structural features of the hormone are consistently predicted. The proposed model for the hormone contains 2 domains dominated by hydrophobic clustering of critical residues within each domain and separated by an exposed linker region. In the prediction of 2 domains with a linker region, the model is similar to that proposed by Fiskin et al., but it differs significantly in other respects. The proposed structural features are apparent in the bovine, human and procine species of hormone.This publication has 24 references indexed in Scilit:
- PREDICTED SECONDARY STRUCTURES OF FOUR PENICILLIN BETA‐LACTAMASES AND A COMPARISON WITH TWO LYSOZYMESInternational Journal of Peptide and Protein Research, 1979
- Analysis of Parathyroid Hormone and Its Fragments in Rat TissuesJournal of Clinical Investigation, 1979
- Prediction of the Secondary Structure of Proteins from their Amino Acid SequencePublished by Wiley ,1979
- Characterisation of a Local Structure in the Synthetic Parathyroid Hormone Fragment 1-34 by 1H Nuclear-Magnetic-Resonance TechniquesEuropean Journal of Biochemistry, 1978
- Cholesterol distribution and movement in the Mycoplasma gallisepticum cell membraneBiochemistry, 1978
- Prediction of chain turns in globular proteins on a hydrophobic basisNature, 1978
- Evidence for topographical analogy between methionine-enkephalin and morphine derivativesBiochemistry, 1977
- Design and Synthesis of Parathyroid Hormone Analogues of Enhanced Biological ActivityEndocrine Research Communications, 1977
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- Bovine Parathyroid Hormone: Minimum Chain Length of Synthetic Peptide Required for Biological ActivityEndocrinology, 1973