Correlation of Solvent Interaction Analysis Signatures with Thermodynamic Properties and In Silico Calculations of the Structural Effects of Point Mutations in Two Proteins

被引：3

作者：

Titus, Amber R. ^{[1
]}

Madeira, Pedro P. ^{[1
,2
]}

Uversky, Vladimir N. ^{[3
,4
]}

Zaslavsky, Boris Y. ^{[1
]}

机构：

[1] Cleveland Diagnost, 3615 Super Ave, Cleveland, OH 44114 USA

[2] Univ Aveiro, Aveiro Inst Mat, Dept Chem, CICECO, P-3810193 Aveiro, Portugal

[3] Univ S Florida, Morsani Coll Med, Dept Mol Med, Tampa, FL 33612 USA

[4] Univ S Florida, Byrd Alzheimers Res Inst, Morsani Coll Med, Tampa, FL 33612 USA

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2024年 / 25卷 / 17期

关键词：

aqueous two-phase system; protein partitioning; solvent interaction analysis; staphylococcal nuclease A; bacteriophage T4 lysozyme; conformational stability; structural signature; ACCESSIBLE SURFACE-AREA; SIGNIFICANT PROSTATE-CANCER; AMINO-ACID-RESIDUES; STABILITY; HYDRATION; ISOPSA; BIOPSY; ASSAY; MEN;

D O I：

10.3390/ijms25179652

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The partition behavior of single and double-point mutants of bacteriophage T4 lysozyme (T4 lysozyme) and staphylococcal nuclease A was examined in different aqueous two-phase systems (ATPSs) and studied by Solvent Interaction Analysis (SIA). Additionally, the solvent accessible surface area (SASA) of modeled mutants of both proteins was calculated. The in silico calculations and the in vitro analyses of the staphylococcal nuclease and T4 lysozyme mutants correlate, indicating that the partition analysis in ATPSs provides a valid descriptor (SIA signature) covering various protein features, such as structure, structural dynamics, and conformational stability.

引用

页数：16

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