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NMR backbone chemical shift assignments of the hvDHFR1:NADPH binary complex.

机译：hvDHFR1：NADPH二元配合物的NMR骨架化学位移分配。

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Extremophiles are the organisms that survive in environments which are inhospitable to other creatures. This thesis made an attempt to understand the enviromental effects, in particular saline, on enzyme structure by using three dimensional NMR. The enzyme DHFR1 from halophile Haloferaxi volcanii is complexed with its cofactor NADPH, and the saline effects on the complex are studied by comparison with its apoenzyme, hvDHFR1. Backbone chemical shift assignments of the hvDHFR1:NADPH complex were attained which can be functional (along with future work) in understanding the effect of salts on enzyme structure, function, and flexibility. A total of 27 amino acids were found to show a significant change upon binding of NADPH and their positions were identified on enzyme complex. The secondary structure of hvDHFR1:NADPH is also predicted and overall global structure is found to be similar with the crystal structure of hvDHFR1 with few changes.

机译：极端微生物是在其他生物不适应的环境中生存的生物。本文试图通过三维核磁共振来了解环境对酶结构的影响，特别是生理盐水。将来自嗜盐嗜盐菌Halferaxi volcanii的酶DHFR1与辅因子NADPH进行复合，并通过与其脱辅酶hvDHFR1的比较研究了盐对复合物的作用。获得了hvDHFR1：NADPH复合物的骨干化学位移，这在理解盐对酶结构，功能和柔韧性的影响方面可以发挥作用（以及未来的工作）。发现总共27个氨基酸在结合NADPH后显示出显着变化，并且在酶复合物上鉴定了它们的位置。还预测了hvDHFR1：NADPH的二级结构，发现总体整体结构与hvDHFR1的晶体结构相似，变化不大。

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作者
Vangala, Karthikeshwar.;
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作者单位

Mississippi State University.;

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授予单位 Mississippi State University.;
学科 Chemistry General.;Chemistry Analytical.;Chemistry Biochemistry.
学位 M.S.
年度 2008
页码 107 p.
总页数 107
原文格式 PDF
正文语种 eng
中图分类化学;生物化学;化学;
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NMR backbone chemical shift assignments of the hvDHFR1:NADPH binary complex.

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