Solution and solid-state circular dichroism analyses of a human salivary proline-rich glycoprotein repeating domain and its subfragments.
Solution and solid-state circular dichroism analyses of a human salivary proline-rich glycoprotein repeating domain and its subfragments.
复制标题
人唾液富含脯氨酸的糖蛋白重复结构域及其亚片段的溶液和固态圆二色性分析。
DOI：
10.1016/0141-8130(93)90018-h
复制
发表时间：
1993
影响因子：
8.2
通讯作者：
Loomis,RE
中科院分区：
文献类型：
--
作者：
Gonzalez,M;Loomis,PM;Loomis,RE
Solution- and solid-state c.d. spectra, as well as surface energetics values, were collected for a series of peptides derived from human salivary proline-rich glycoprotein (PRG). The acronyms and sequences for these peptides are as follows: PRG9-2 = NH2-G(1)-P(2)-CONH2, PRG9-3 = NH2-G(1)-P(2)-P(3)-CONH2, PRG9-4 = NH2-G(1)-P(2)-P(3)-P(4)-CONH2, PRG9-5 = NH2-G(1)-P(2)-P(3)-P(4)-H(5)-CONH2, PRG9-6 = NH2-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-CONH2, PRG9-7 = NH2-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-CONH2, PRG9-8 = NH2-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-K(8)-CONH2, and PRG9-9 = NH2-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-K(8)-P(9)-CONH2. The presence of stable poly-l-proline II-like ‘mini’ helices in the solution state was found to be dependent on peptide chain length, pH, salt, and organic solvent type. Other conformational features such as kinks and β-/γ-turns were also found in the larger peptides. Solid-state peptide conformations were not necessarily related to their solution-state counterparts. Poly-l-proline II-like ‘mini’ helices, kinks, and β-/γ-turns were similarly found in the various substrate-bound PRG9 peptides. Surface energetics parameters suggested specific orientations for PRG9 peptides and their constituent acids and homopolymers.
