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Stereochemistry of the Interaction between Methionine Sulfur and the Protein Core
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O. Carugo
Veröffentlicht/Copyright:
1. Juni 2005
Abstract
The stereochemical features of the interaction between the sulfur atom of methionine residues and surrounding atoms are examined on a large set of known protein crystal structures. It appears that the minimum energy conformations observed in small molecule crystals are not observed within the protein core. This suggests that these interactions are either of little intensity, though they might contribute to regulate the protein physiological behavior, or physicochemically different from their counterpart in small molecule crystals.
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Published Online: 2005-06-01
Published in Print: 1999-04-01
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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Artikel in diesem Heft
- Protein Kinase C-α Produces Reciprocal Effects on the Phorbol Ester Stimulated Tyrosine Phosphorylation of a 50 kDa Kinase in Jurkat Cells
- Growth- and Development-Dependent Expression of Gangliosides in Rat Hepatocytes and Liver Tissues
- Regulated Phosphorylation of the Gal4p Inhibitor Gal80p of <I>Kluyveromyces lactis</I> Revealed by Mutational Analysis
- The WW Domain of Dystrophin Requires EF-Hands Region to Interact with β-Dystroglycan
- Purification and MALDI-MS Characterization of Stressin, a Stress-Associated Glycoprotein
- Direct Selection of EGF Mutants Displayed on Filamentous Phage Using Cells Overexpressing EGF Receptor
- Refolding Studies on the Tetrameric Loop Deletion Mutant RM6 of ROP Protein
- Secretion of Protease Nexin-II/Amyloid β Protein Precursor by Human Colorectal Carcinoma Cells and Its Modulation by Cytokines/Growth Factors and Proteinase Inhibitors
- Isolation and Primary Structure of the CCI Papain-Like Cysteine Proteinases from the Latex of Carica candamarcensis Hook
- Identification of SLPI (Secretory Leukocyte Protease Inhibitor) in Human Mast Cells Using Immunohistochemistry and In Situ Hybridisation
- Stereochemistry of the Interaction between Methionine Sulfur and the Protein Core
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