FLUORINATED AMINO ACIDS IN HELIX-COIL TRANSITIONS

螺旋-螺旋转变中的氟化氨基酸

• 批准号: 7723855
• 负责人: RICHARD P CHENG
• 金额: $ 0.26万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-06-01 至 2009-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7723855
• 关键词: Accounting; Amino Acids; Biotechnology; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Helix (Snails); Hydrophobicity; Institution; Nanotechnology; Peptides; Proteins; Research; Research Personnel; Resources; Source; United States National Institutes of Health; ear helix

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Fluorinated amino acids have applications in both nanotechnology and biotechnology. Their appeal arises from their stabilizing effect on proteins, but the origin of this enhanced stability is not well understood. It has been suggested that the increased hydrophobicity of fluorinated amino acids may account for the increased stability of helical peptides that include them, because the ¿G gained in hydrophobicity is similar to that gained in the overall stability of these peptides. However, the helical propensities of fluorinated amino acids are much lower than their natural counterparts, leading one to believe that the increased stability originates from more that just the hydrophobic effect.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 含氟氨基酸在纳米技术和生物技术中都有应用。它们的吸引力来自于它们对蛋白质的稳定作用，但这种增强的稳定性的起源还不清楚。有人认为，氟化氨基酸的疏水性增加可能是包括它们的螺旋肽的稳定性增加的原因，因为疏水性获得的Δ G与这些肽的总体稳定性获得的Δ G相似。然而，氟化氨基酸的螺旋倾向比它们的天然对应物低得多，这使得人们相信增加的稳定性不仅仅来自疏水作用。