scholarly journals PEGylation near a Patch of Nonpolar Surface Residues Increases the Conformational Stability of the WW Domain

2019 ◽  
Vol 85 (3) ◽  
pp. 1725-1730
Author(s):  
Steven R. E. Draper ◽  
Dallin S. Ashton ◽  
Benjamin M. Conover ◽  
Anthony J. Carter ◽  
Kimberlee L. Stern ◽  
...  
Keyword(s):  
Conformational Stability ◽  
Ww Domain

scholarly journals Stapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect

2018 ◽  
Vol 16 (46) ◽  
pp. 8933-8939 ◽  
Author(s):  
Qiang Xiao ◽  
Natalie A. Bécar ◽  
Nathaniel P. Brown ◽  
Mason S. Smith ◽  
Kimberlee L. Stern ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Conformational Stability ◽  
Side Chains ◽  
Primary Sequence ◽  
Ww Domain ◽  
Entropic Effect

PEGylation + stapling contributes more to conformational stability when the two linked sites are close in tertiary structure but far apart in primary sequence.

Impact of Site-Specific PEGylation on the Conformational Stability and Folding Rate of the Pin WW Domain Depends Strongly on PEG Oligomer Length

2013 ◽  
Vol 24 (5) ◽  
pp. 796-802 ◽  
Author(s):  
Brijesh K. Pandey ◽  
Mason S. Smith ◽  
Chad Torgerson ◽  
Paul B. Lawrence ◽  
Sam S. Matthews ◽  
...  
Keyword(s):  
Conformational Stability ◽  
Folding Rate ◽  
Site Specific ◽  
Ww Domain

Insights into the Structural Features, Conformational Stability and Functional Activity of the Olneya tesota PF2 Lectin

2020 ◽  
Vol 27 ◽  
Author(s):  
Edgar Acedo-Espinoza ◽  
Irlanda Lagarda-Diaz ◽  
Rosina Cabrera ◽  
Ana M. Guzman-Partida ◽  
Amir Maldonado-Arce ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Proteolytic Enzymes ◽  
Conformational Stability ◽  
Structural Features ◽  
Beta Sheets ◽  
Hemagglutinating Activity ◽  
Effect Of Temperature ◽  
Hydrodynamic Diameter ◽  
Bioinformatic Tools ◽  
Structural Levels

Background: The O. tesota lectin PF2 is a tetrameric protein with subunits of 33 kDa that recognizes only complex carbohydrates, resistant to proteolytic enzymes and has insecticidal activity against Phaseolus beans pest. Objective: To explore PF2 lectin features at different protein structural levels and to evaluate the effect of temperature and pH on its functionality and conformational stability. Methods: PF2 lectin was purified by affinity chromatography. Its primary structure was resolved by mass spectrometry and analyzed by bioinformatic tools, including its tertiary structure homology modeling. The effect of temperature and pH on its conformational traits and stability was addressed by dynamic light scattering, circular dichroism, and intrinsic fluorescence. The hemagglutinating activity was evaluated using a suspension of peripheral blood erythrocytes. Results: The proposed PF2 folding comprises a high content of beta sheets. At pH 7 and 25 °C, the hydrodynamic diameter (Dh) was found to be 12.3 nm which corresponds to the oligomeric native state of PF2 lectin. Dh increased under the other evaluated pH and temperature conditions, suggesting protein aggregation. At basic pH, PF2 exhibited low conformational stability. The native PF2 (pH 7) retained its full hemagglutinating activity up to 45 °C and exhibited one transition state with a melting temperature of 76.8 °C. Conclusion: PF2 showed distinctive characteristics found in legume lectins. The pH influences the functionality and conformational stability of the protein. PF2 lectin displayed a relatively narrow thermostability to the loss of secondary structure and hemagglutinating activity.

Conformational Stability, FMO, NMR, MEP and NBO Analysis of 2,5-Di-methyl-2,5-bis(methylthio)-1,4-dithiane and Dimethoxy compounds by DFT Approach

2021 ◽  
Vol 17 ◽  
Author(s):  
Nasrin Masnabadi
Keyword(s):  
Computational Methods ◽  
Electrostatic Potential ◽  
Conformational Stability ◽  
Nbo Analysis ◽  
Dft Methods ◽  
Geometrical Properties ◽  
Stereoelectronic Effect ◽  
Nmr Parameters ◽  
Electron Transfers ◽  
Stability Energy

Abstract: Conformational behaviors of 2,5-dimethoxy-2,5-dimethyl-1,4-dithiane (compound 1) and 2,5-dimethyl-2,5-bis (methylthio)-1,4-dithiane (compound 2) investigated by computational methods including B3LYP/6-311+G** and M06-2X/6-311+G** levels of theory and NBO analysis. The stereoelectronic effect of axial, axial (ax, ax) and equatorial, equa-torial (eq, eq) conformations were studied using NBO analysis. Using NBO analysis, the values of the stereoelectronic effects were calculated through the energy of stability associated with the electron transfers of compounds 1 and 2. The results showed that the eq, eq conformations of the studied compounds were more stable than their corresponding ax, ax conformations, and LP2X→σS1-C2 and LP2S→σ*C2-X electron transfers play important roles in the conformational be-havior of the studied compounds. The main purpose of the present work was to study the effects of stereoelectronic inter-actions and steric on the conformational superiority of the di-methoxy (compound 1) and di-thiomethyl compounds (com-pound 2). Thus, the values of resonance stability energy, non-diagonal elements, and orbital populations were investigated. Also, active electrophilic and nucleophilic centers were identified using fronting orbitals analysis obtained by DFT methods. The electrostatic potential maps of the title compounds were investigated at the B3LYP/6-311+G* level of theory. All of the NMR parameters and geometrical properties of both compounds were determined in this study.

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