Water hydrogen bonding (H-bonding) to α-helical transmembrane (TM) peptides is fundamental to better understand the behavior and function of α-helical peptides, disease pathways, and the development of new drugs. Deep-UV resonance Raman (dUVRR) spectroscopy is a non-destructive technique amenable to both lipophilic and aqueous environments, which is an excellent and convenient approach for studying water H-bonding (or water accessibility) to α-helical TM peptides in a membrane mimicking environment. The dUVRR results indicate that water molecules can access the lipid membrane and form H-bonds with carbonyl groups along α-helical backbones. Raman bands at ~1,629 and ~1,672 cm⁻¹ can be used to monitor the hydration and dehydration conditions along TM α-helices. Two bands at ~1,300 and ~1,340 cm⁻¹ are also potential characteristic features of the dehydration and hydration along the α-helices in a membrane environment.

中文翻译：

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脂质体中水合和脱水模型α-螺旋跨膜肽的深紫外共振拉曼光谱

水与 α-螺旋跨膜 (TM) 肽的氢键 (H-bonding) 是更好地了解 α- 螺旋肽的行为和功能、疾病途径和新药开发的基础。深紫外共振拉曼 (dUVRR) 光谱是一种非破坏性技术，适用于亲脂性和水性环境，是研究膜中水 H 键（或水可及性）与 α-螺旋 TM 肽的一种出色且方便的方法模仿环境。dUVRR 结果表明水分子可以进入脂质膜并与沿α-螺旋骨架的羰基形成氢键。~1,629 和 ~1,672 cm ^-1的拉曼谱带可用于监测沿 TM α-螺旋的水合和脱水条件。~1,300 和 ~1,340 cm ^{-1的两个波段} 也是膜环境中沿α-螺旋脱水和水合的潜在特征。