Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long-range hydrophobic interactions.
Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long-range hydrophobic interactions.
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DOI：
10.1002/prot.22605
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发表时间：
2010-02-15
影响因子：
2.9
通讯作者：
Scheraga, Harold A.
中科院分区：
文献类型：
--
作者：
Lewandowska, Agnieszka;Oldziej, Stanislaw;Liwo, Adam;Scheraga, Harold A.
使用不同温度下的 CD、NMR 光谱和差示扫描量热法研究了源自链球菌免疫球蛋白结合蛋白 G B3 结构域的 C 端 β 发夹的 20 个残基肽 IG(42–61)。与迄今为止研究的其他相关肽不同，该肽在 DSC 测量中显示出两个热容峰（扫描速率为 1.5 度/分钟，肽浓度为 0.07mM），这表明存在三态折叠/展开过程。 DSC 和 NMR 测量结果表明，形成了疏水相互作用的动态网络，稳定了结构，该结构在较宽的温度范围（283 – 313 K）下类似于 β-发夹形状。我们的结果表明，IG(42–61) 具有组织良好的三维结构，通过长程疏水相互作用（Tyr50 … Phe57 和 Trp48 … Val59）在 T = 283 K 和（Trp48 … Val59）在 305 和 313 K 稳定。还讨论了 β-发夹折叠和解折叠的机制，以及肽长度对其构象特性的影响。
A 20-residue peptide, IG(42–61), derived from the C-terminal β-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptoccocus was studied using CD, NMR spectroscopy at various temperatures and by differential scanning calorimetry. Unlike other related peptides studied so far, this peptide displays two heat capacity peaks in DSC measurements (at a scanning rate of 1.5 deg/min at a peptide concentration of 0.07mM) which suggests a three-state folding/unfolding process. The results from DSC and NMR measurements suggest the formation of a dynamic network of hydrophobic interactions stabilizing the structure, which resembles a β-hairpin shape over a wide range of temperatures (283 – 313 K). Our results show that IG(42–61) possesses a well-organized three-dimensional structure stabilized by long-range hydrophobic interactions (Tyr50 ··· Phe57 and Trp48 ··· Val59) at T = 283 K and (Trp48 ··· Val59) at 305 and 313 K. The mechanism of β-hairpin folding and unfolding, as well as the influence of peptide length on its conformational properties, are also discussed.
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