Volume and sound velocity changes accompanying the α-helix to β-form and coil to α-helix transitions in aqueous solution
✍ Scribed by Hajime Noguchi; Jen Tsi Yang
- Book ID
- 102761082
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1971
- Tongue
- English
- Weight
- 621 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The volume increment per amino acid residue for the a-helix to @-form transition of uncharged poly-clysine in aqueous solution was 3.8 ml in water and 4.3 ml in 0.2M and 1M NaBr solutions at 26"C, respectively. The sound velocity of the polymer solution was greater with the a-helix than with the @-form, but the difference was less in dilute salt solutions and disappeared in 1 or 2M NaBr solution. Thus, the @ poly-clysine solution was slightly more compressible than the a-polymer solution, but this difference was diminished with increasing salt concentration. Both the volume change and the change in adiabatic compressibility of the polymer solution suggest that hydrophobic interactions among the lysyl groups in the 8-form reduce the amount of "icebergs" surrounding the polymer molecules as compared with the amount originally present with the a-helix. The coil-to-helii transition of poly-L-glutamic acid in aqueous solution was also accompanied by a decrease in sound velocity. This can be attributed to the reduction of the water of hydration which is less compressible than free water.
📜 SIMILAR VOLUMES
## Abstract Thermodynamic stability in polypeptides is described using a novel Distance Constraint Model (DCM). Here, microscopic interactions are represented as constraints. A topological arrangement of constraints define a mechanical framework. Each constraint in the framework is associated with