Cis/trans heterogeneity of Gln30-Pro31 peptide bond determines whether a 79-residue fragment of staphylococcal nuclease self-associates.
Cis/trans heterogeneity of Gln30-Pro31 peptide bond determines whether a 79-residue fragment of staphylococcal nuclease self-associates.
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Gln30-Pro31 肽键的顺/反异质性决定了葡萄球菌核酸酶的 79 个残基片段是否自缔合。
DOI：
10.1016/j.bbrc.2005.01.155
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发表时间：
2005
影响因子：
3.1
通讯作者：
Jinfeng Wang
中科院分区：
文献类型：
--
作者：
X. Wang;Y. Tong;Jinfeng Wang
用远紫外圆二色谱、分子排阻色谱和异谱多维核磁共振研究了葡萄球菌核酸酶SNase 79的自缔合反应。大量SNase 79处于自缔合状态，而少量SNase 79基本上处于单体状态。序列区Thr 13-Val 39负责SNase 79的结合界面。Gln 30-Pro31的反式构象可能使氨基酸残基Tyr 27-Gln 30成为折叠成核位点，并导致SNase 79的Thr 13-Val 39片段呈现天然β折叠构象，从而导致SNase 79的自缔合。SNase 79的片段Thr 13-Val 39的非天然构象与X-脯氨酰键Gln 30-Pro31的顺式构象相关，可能将SNase 79从可溶性聚集体中排除。
The self-association reaction of a 79-residue fragment of staphylococcal nuclease (SNase79) was studied by far-UV CD, size-exclusion chromatography, and heteronuclear multidimensional NMR spectroscopy. A large population of SNase79 is in self-associated state while a small population of SNase79 is essentially in a monomeric state. The sequence region Thr13-Val39 is responsible for association interface of SNase79. The trans-conformation of X-prolyl bond Gln30-Pro31 may make residues Tyr27-Gln30, serve as a folding nucleation site, and lead the segment Thr13-Val39 of SNase79 to adopt a native-like β-sheet conformation, which results in the self-association of SNase79. The non-native conformation of the segment Thr13-Val39 of SNase79 associated with the cis-conformation of X-prolyl bond Gln30-Pro31 may preclude SNase79 from the soluble aggregates.
影响因子：
2.9
作者：
Wang,JF;Hinck,AP;Loh,SN;Markley,JL
通讯作者：
Markley,JL