Hydrogen Bonding on the Ice-Binding Face of a β-Helical Antifreeze Protein Indicated by Amide Proton NMR Chemical Shifts
| Autor: | Steffen P. Graether, Brian D. Sykes, Margaret E Daley |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Protein Conformation
Molecular Sequence Data Amide proton Biochemistry Protein Structure Secondary chemistry.chemical_compound Antifreeze protein Antifreeze Proteins Amide Animals Organic chemistry Peptide bond Amino Acid Sequence Threonine Tenebrio Nuclear Magnetic Resonance Biomolecular Nitrogen Isotopes Hydrogen bond Chemical shift Ice Temperature Hydrogen Bonding Amides Crystallography Ice binding chemistry Insect Proteins Thermodynamics Protons Protein Binding |
| Zdroj: | Biochemistry. 43:13012-13017 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi0488092 |
| Popis: | The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical antifreeze protein from Tenebrio molitor are examined to determine their hydrogen bonding state in solution. The temperature-dependent chemical shift behavior of the amides in T. molitor antifreeze protein varies widely throughout the protein backbone; however, very subtle effects of hydrogen bonding can be distinguished using a plot of chemical shift deviation (CSD) versus the backbone amide chemical shift temperature gradient (Deltadelta/DeltaT). We show that differences between the two ranks of ice-binding threonine residues on the surface of the protein indicate that threonine residues in the left-hand rank participate in intrastrand hydrogen bonds that stabilize the flat surface required for optimal ice binding. |
| Databáze: | OpenAIRE |
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