变性状态下的电荷-电荷相互作用影响核糖核酸酶Sa的折叠动力学。
Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.
作者信息
Trefethen Jared M, Pace C Nick, Scholtz J Martin, Brems David N
机构信息
Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-1114, USA.
出版信息
Protein Sci. 2005 Jul;14(7):1934-8. doi: 10.1110/ps.051401905. Epub 2005 Jun 3.
Abstract
Gaining a better understanding of the denatured state ensemble of proteins is important for understanding protein stability and the mechanism of protein folding. We studied the folding kinetics of ribonuclease Sa (RNase Sa) and a charge-reversal variant (D17R). The refolding kinetics are similar, but the unfolding rate constant is 10-fold greater for the variant. This suggests that charge-charge interactions in the denatured state and the transition state ensembles are more favorable in the variant than in RNase Sa, and shows that charge-charge interactions can influence the kinetics and mechanism of protein folding.
摘要
更好地理解蛋白质的变性态系综对于理解蛋白质稳定性和蛋白质折叠机制至关重要。我们研究了核糖核酸酶Sa（RNase Sa）和一个电荷反转变体（D17R）的折叠动力学。复性动力学相似，但该变体的解折叠速率常数比RNase Sa大10倍。这表明在变性态和过渡态系综中，该变体的电荷-电荷相互作用比RNase Sa更有利，并且表明电荷-电荷相互作用可以影响蛋白质折叠的动力学和机制。
相似文献
1
Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.变性状态下的电荷-电荷相互作用影响核糖核酸酶Sa的折叠动力学。
Protein Sci. 2005 Jul;14(7):1934-8. doi: 10.1110/ps.051401905. Epub 2005 Jun 3.
2
Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.电荷-电荷相互作用影响变性态系综并有助于蛋白质稳定性。
Protein Sci. 2000 Jul;9(7):1395-8. doi: 10.1110/ps.9.7.1395.
3
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.通过核磁共振监测氢交换研究核糖核酸酶 Sa 的构象稳定性。
Biochemistry. 2005 May 31;44(21):7644-55. doi: 10.1021/bi050142b.
4
Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2).电荷-电荷相互作用是核糖核酸酶Sa（pI = 3.5）和一种碱性变体（pI = 10.2）中可电离基团pK值的关键决定因素。
J Mol Biol. 2003 Jan 31;325(5):1077-92. doi: 10.1016/s0022-2836(02)01273-1.
5
Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3.核糖核酸酶Sa、Sa2和Sa3的构象稳定性及折叠热力学
J Mol Biol. 1998 May 29;279(1):271-86. doi: 10.1006/jmbi.1998.1760.
6
Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.单个色氨酸残基对核糖核酸酶Sa荧光及稳定性的贡献
Biophys J. 2004 Dec;87(6):4036-47. doi: 10.1529/biophysj.104.050377. Epub 2004 Sep 17.
7
Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme.普通型酰基磷酸酶折叠的热力学与动力学：与高度同源的肌肉同工酶的比较。
Biochemistry. 1999 Feb 16;38(7):2135-42. doi: 10.1021/bi9822630.
8
Nonnative electrostatic interactions can modulate protein folding: molecular dynamics with a grain of salt.非天然静电相互作用可调节蛋白质折叠：带点盐味的分子动力学
J Mol Biol. 2009 Oct 23;393(2):527-42. doi: 10.1016/j.jmb.2009.08.010. Epub 2009 Aug 13.
9
The role of protein stability, solubility, and net charge in amyloid fibril formation.蛋白质稳定性、溶解性和净电荷在淀粉样纤维形成中的作用。
Protein Sci. 2003 Oct;12(10):2374-8. doi: 10.1110/ps.03152903.
10
A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins.一种用于处理蛋白质未折叠状态下残余电荷-电荷相互作用的高斯链模型。
Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3569-74. doi: 10.1073/pnas.052030599. Epub 2002 Mar 12.
引用本文的文献
1
Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.含序列差异的三螺旋束中变性状态构象偏向定位于转角和螺旋帽残基附近。
Biochemistry. 2021 Oct 19;60(41):3071-3085. doi: 10.1021/acs.biochem.1c00400. Epub 2021 Oct 4.
2
Ion-ion interactions in the denatured state contribute to the stabilization of CutA1 proteins.离子-离子相互作用在变性状态下有助于 CutA1 蛋白的稳定。
Sci Rep. 2018 May 16;8(1):7613. doi: 10.1038/s41598-018-25825-7.
3
Microbial ribonucleases (RNases): production and application potential.微生物核糖核酸酶（RNases）：生产及应用潜力
World J Microbiol Biotechnol. 2015 Dec;31(12):1853-62. doi: 10.1007/s11274-015-1945-8. Epub 2015 Oct 3.
4
Energetically significant networks of coupled interactions within an unfolded protein.伸展蛋白质内能量显著的耦合相互作用网络。
Proc Natl Acad Sci U S A. 2014 Aug 19;111(33):12079-84. doi: 10.1073/pnas.1402054111. Epub 2014 Aug 6.
5
Rational modification of protein stability by targeting surface sites leads to complicated results.通过靶向表面位点来合理修饰蛋白质稳定性会导致复杂的结果。
Proc Natl Acad Sci U S A. 2013 Jul 9;110(28):11337-42. doi: 10.1073/pnas.1222245110. Epub 2013 Jun 24.
6
Increased alkalotolerant and thermostable ribonuclease (RNase) production from alkaliphilic Streptomyces sp. M49-1 by optimizing the growth conditions using response surface methodology.利用响应面法优化生长条件，提高嗜堿放线菌 M49-1 产堿性和耐热型核糖核酸酶（RNase）的能力。
World J Microbiol Biotechnol. 2013 Sep;29(9):1625-33. doi: 10.1007/s11274-013-1325-1. Epub 2013 Mar 27.
7
Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured-state ensemble of iso-1-cytochrome c.芳香族氨基酸与亮氨酸和脯氨酸诱导同工型 1-细胞色素 c 去折叠态集合体中残留结构的倾向性。
J Mol Biol. 2010 Nov 5;403(4):495-504. doi: 10.1016/j.jmb.2010.09.004. Epub 2010 Sep 17.
8
Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins.尿素变性状态集合包含广泛的二级结构，在疏水蛋白中增加。
Protein Sci. 2010 May;19(5):929-43. doi: 10.1002/pro.370.
9
Effective approach for calculations of absolute stability of proteins using focused dielectric constants.利用聚焦介电常数计算蛋白质绝对稳定性的有效方法。
Proteins. 2009 Nov 15;77(3):670-84. doi: 10.1002/prot.22481.
10
Thermally denatured state determines refolding in lipase: mutational analysis.热变性状态决定脂肪酶的重折叠：突变分析
Protein Sci. 2009 Jun;18(6):1183-96. doi: 10.1002/pro.126.
本文引用的文献
1
Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding.对组氨酸点突变体的pH依赖性折叠和稳定性进行分析，可以对蛋白质折叠的变性状态和过渡态进行表征。
J Mol Biol. 2005 Jan 7;345(1):163-73. doi: 10.1016/j.jmb.2004.10.023.
2
Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.单个色氨酸残基对核糖核酸酶Sa荧光及稳定性的贡献
Biophys J. 2004 Dec;87(6):4036-47. doi: 10.1529/biophysj.104.050377. Epub 2004 Sep 17.
3
Effect of salt on the urea-unfolded form of barstar probed by m value measurements.通过m值测量探究盐对巴司星尿素展开形式的影响。
Biochemistry. 2004 Sep 14;43(36):11393-402. doi: 10.1021/bi049320b.
4
Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state.蛋白质折叠中非天然相互作用的热力学和动力学：一个单点突变通过调节变性状态下的非天然相互作用显著稳定了L9的N端结构域。
J Mol Biol. 2004 May 7;338(4):827-37. doi: 10.1016/j.jmb.2004.02.073.
5
The kinetic pathway of folding of barnase.核糖核酸酶 barnase 的折叠动力学途径。
J Mol Biol. 2003 Oct 10;333(1):169-86. doi: 10.1016/j.jmb.2003.08.024.
6
The present view of the mechanism of protein folding.目前关于蛋白质折叠机制的观点。
Nat Rev Mol Cell Biol. 2003 Jun;4(6):497-502. doi: 10.1038/nrm1126.
7
The effect of net charge on the solubility, activity, and stability of ribonuclease Sa.净电荷对核糖核酸酶Sa的溶解度、活性和稳定性的影响。
Protein Sci. 2001 Jun;10(6):1206-15. doi: 10.1110/ps.440101.
8
Linear extrapolation method of analyzing solvent denaturation curves.分析溶剂变性曲线的线性外推法
Proteins. 2000;Suppl 4:1-7. doi: 10.1002/1097-0134(2000)41:4+<1::aid-prot10>3.3.co;2-u.
9
Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.电荷-电荷相互作用影响变性态系综并有助于蛋白质稳定性。
Protein Sci. 2000 Jul;9(7):1395-8. doi: 10.1110/ps.9.7.1395.
10
Rational modification of protein stability by the mutation of charged surface residues.通过带电荷表面残基的突变对蛋白质稳定性进行合理修饰。
Biochemistry. 2000 Feb 8;39(5):872-9. doi: 10.1021/bi992091m.
Zotero 插件