The intramolecular helix backbone C O ---H-N hydrogen Ž . bonding energies in poly L-alanine ␣ helices have been estimated both in vacuum and in an aqueous environment using the parameter sets of five of the most commonly used force fields for modeling biomolecules, namely AMBER, CHARMM, ECEPP, GROM
✦ LIBER ✦
pH dependence of hydrogen bond strengths in myoglobin α-helices
✍ Scribed by V. Le Tilly; O. Sire; P.T.T. Wong; B. Alpert
- Book ID
- 103036070
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 246 KB
- Volume
- 192
- Category
- Article
- ISSN
- 0009-2614
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✦ Synopsis
Hydrogen bond strengths inside the azidometmyoglobin molecule in solution were investigated through a high-pressure Fourier transform infrared study of the amide I absorption band. This work gives strong indications in support of a variation of the strength of the hydrogen bonds inside the myoglobin helices with the pH. The perturbations on the intramolecular interactions induced by the protons of the solvent could be a key to the understanding of protein activity.
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