短链胶原蛋白模型多肽（L-脯氨酰-L-脯氨酰甘氨酰）5在水性介质中的动力学和水合行为
Dynamics and hydration behavior of a short collagen model polypeptide, (L-prolyl-L-prolylglycyl)5, in aqueous media.
作者信息
Shikata Toshiyuki, Yoshida Nao, Minakawa Ayako, Okuyama Kenji
出版信息
J Phys Chem B. 2009 Jul 9;113(27):9055-8. doi: 10.1021/jp904568r.
A short collagen model polypeptide, (l-prolyl-l-prolylglycyl)(5) (PPG5), behaves as a fully dissociated flexible zwitterionic polymer chain in pure water. Its first and third normal modes of chain conformational fluctuation were detected as distinct dielectric relaxation modes. Addition of acetic acid at 30 mM to an aqueous solution of PPG5 effectively suppressed the overall relaxation strength by protonation of the carboxy termini of the polypeptide. Furthermore, the hydration number per PPG5 molecule was determined to be 130 by dielectric relaxation (DR) spectroscopy over a frequency range from 1 MHz to 20 GHz; this value was not affected by the addition of acetic acid.
一种短的胶原蛋白模型多肽，(l-脯氨酰-l-脯氨酰甘氨酰)(5)（PPG5），在纯水中表现为完全解离的柔性两性离子聚合物链。其链构象波动的第一和第三正常模式被检测为不同的介电弛豫模式。向PPG5水溶液中添加30 mM的乙酸通过多肽羧基末端的质子化有效地抑制了整体弛豫强度。此外，通过介电弛豫（DR）光谱在1 MHz至20 GHz的频率范围内确定每个PPG5分子的水合数为130；该值不受乙酸添加的影响。
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