Noncovalent Carbon-Bonding Interactions in Proteins
| Autor: | Dipak Kumar Sahoo, Suman Bhaumik, Amol Chandrakar, Himansu S. Biswal, V. Rao Mundlapati, Subhrakant Jena |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 02 engineering and technology 010402 general chemistry 01 natural sciences Catalysis Nucleobase Hydrophobic effect chemistry.chemical_compound Computational chemistry Non-covalent interactions Animals Horses chemistry.chemical_classification Halogen bond 010405 organic chemistry Hydrogen bond Myoglobin Biomolecule Photodissociation Proteins Hydrogen Bonding General Medicine General Chemistry 021001 nanoscience & nanotechnology Carbon 0104 chemical sciences chemistry Quantum Theory Thermodynamics 0210 nano-technology Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Angewandte Chemie (International ed. in English). 57(50) |
| ISSN: | 1521-3773 |
| Popis: | Carbon bonds (C-bonds) are the highly directional noncovalent interactions between carbonyl-oxygen acceptors and sp3 -hybridized-carbon σ-hole donors through n→σ* electron delocalization. We have shown the ubiquitous existence of C-bonds in proteins with the help of careful protein structure analysis and quantum calculations, and have precisely determined C-bond energies. The importance of conventional noncovalent interactions such as hydrogen bond (H-bonds) and halogen bond (X-bonds) in the structure and function of biological molecules are well established, while carbon bonds C-bonds have still to be recognized. We have shown that C-bonds are present in proteins, contribute enthalpically to the overall hydrophobic interaction and play a significant role in the photodissociation mechanism of myoglobin and the binding of nucleobases to proteins. |
| Databáze: | OpenAIRE |
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