scholarly journals SAAFEC: Predicting the Effect of Single Point Mutations on Protein Folding Free Energy Using a Knowledge-Modified MM/PBSA Approach

2016 ◽  
Vol 17 (4) ◽  
pp. 512 ◽  
Author(s):  
Ivan Getov ◽  
Marharyta Petukh ◽  
Emil Alexov
Keyword(s):  
Free Energy ◽  
Protein Folding ◽  
Single Point ◽  
Point Mutations ◽  
Single Point Mutations ◽  
Folding Free Energy

scholarly journals Predicting folding free energy changes upon single point mutations

2012 ◽  
Vol 28 (5) ◽  
pp. 664-671 ◽  
Author(s):  
Zhe Zhang ◽  
Lin Wang ◽  
Yang Gao ◽  
Jie Zhang ◽  
Maxim Zhenirovskyy ◽  
...  
Keyword(s):  
Free Energy ◽  
Single Point ◽  
Point Mutations ◽  
Single Point Mutations ◽  
Folding Free Energy

Free energy calculations of A2Aadenosine receptor mutation effects on agonist binding

2015 ◽  
Vol 51 (17) ◽  
pp. 3522-3525 ◽  
Author(s):  
Henrik Keränen ◽  
Johan Åqvist ◽  
Hugo Gutiérrez-de-Terán
Keyword(s):  
Free Energy ◽  
Ligand Binding ◽  
Single Point ◽  
Point Mutations ◽  
Free Energy Calculations ◽  
Computational Scheme ◽  
Agonist Binding ◽  
Energy Calculations ◽  
Single Point Mutations

A general computational scheme to evaluate the effects of single point mutations on ligand binding is reported.

Cupin Variants as Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes

2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Miho Yuasa ◽  
Yosuke Nishikawa ◽  
Genji Kurisu ◽  
Shinobu Itoh ◽  
...  
Keyword(s):  
Michael Addition ◽  
In Silico ◽  
Addition Reaction ◽  
Single Point ◽  
Point Mutations ◽  
Unsaturated Ketone ◽  
Michael Addition Reaction ◽  
Beta Barrel ◽  
Cupin Superfamily ◽  
Single Point Mutations

Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantio-selective Michael addition reaction of nitroalkanes to an α,β-unsaturated ketone. Moreover, in silico substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.

Single-Point Mutations in Qβ Virus-like Particles Change Binding to Cells

2021 ◽  
Author(s):  
Marisa L. Martino ◽  
Stephen N. Crooke ◽  
Marianne Manchester ◽  
M.G. Finn
Keyword(s):  
Single Point ◽  
Point Mutations ◽  
Virus Like Particles ◽  
Single Point Mutations

MinD directly interacting with FtsZ at the H10 helix suggests a model for robust activation of MinC to destabilize FtsZ polymers

2017 ◽  
Vol 474 (18) ◽  
pp. 3189-3205 ◽  
Author(s):  
Ashoka Chary Taviti ◽  
Tushar Kant Beuria
Keyword(s):  
Cell Division ◽  
Single Point ◽  
Point Mutations ◽  
Direct Interaction ◽  
Ring Formation ◽  
Z Ring ◽  
Single Point Mutations ◽  
Biochemical Analyses ◽  
Ftsz Assembly ◽  
The Mind

Cell division in bacteria is a highly controlled and regulated process. FtsZ, a bacterial cytoskeletal protein, forms a ring-like structure known as the Z-ring and recruits more than a dozen other cell division proteins. The Min system oscillates between the poles and inhibits the Z-ring formation at the poles by perturbing FtsZ assembly. This leads to an increase in the FtsZ concentration at the mid-cell and helps in Z-ring positioning. MinC, the effector protein, interferes with Z-ring formation through two different mechanisms mediated by its two domains with the help of MinD. However, the mechanism by which MinD triggers MinC activity is not yet known. We showed that MinD directly interacts with FtsZ with an affinity stronger than the reported MinC–FtsZ interaction. We determined the MinD-binding site of FtsZ using computational, mutational and biochemical analyses. Our study showed that MinD binds to the H10 helix of FtsZ. Single-point mutations at the charged residues in the H10 helix resulted in a decrease in the FtsZ affinity towards MinD. Based on our findings, we propose a novel model for MinCD–FtsZ interaction, where MinD through its direct interaction with FtsZ would trigger MinC activity to inhibit FtsZ functions.

scholarly journals Single-point mutations of hepatitis C virus NS3 that impair p53 interaction and anti-apoptotic activity of NS3

2006 ◽  
Vol 340 (3) ◽  
pp. 792-799 ◽  
Author(s):  
Motofumi Tanaka ◽  
Motoko Nagano-Fujii ◽  
Lin Deng ◽  
Satoshi Ishido ◽  
Kiyonao Sada ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Single Point ◽  
Point Mutations ◽  
Single Point Mutations ◽  
Apoptotic Activity
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