scispace - formally typeset
Open AccessJournal ArticleDOI

FoldX as Protein Engineering Tool: Better Than Random Based Approaches?

TLDR
In this review different algorithms for the prediction of beneficial mutation sites to enhance protein stability are summarized and the advantages and disadvantages of FoldX are highlighted.
Abstract
Improving protein stability is an important goal for basic research as well as for clinical and industrial applications but no commonly accepted and widely used strategy for efficient engineering is known. Beside random approaches like error prone PCR or physical techniques to stabilize proteins, e.g. by immobilization, in silico approaches are gaining more attention to apply target-oriented mutagenesis. In this review different algorithms for the prediction of beneficial mutation sites to enhance protein stability are summarized and the advantages and disadvantages of FoldX are highlighted. The question whether the prediction of mutation sites by the algorithm FoldX is more accurate than random based approaches is addressed.

read more

Citations
More filters
Journal ArticleDOI

Utility of B-Factors in Protein Science: Interpreting Rigidity, Flexibility, and Internal Motion and Engineering Thermostability.

TL;DR: This review begins with analyses of early protein studies which suggested that B-factors, available from the Protein Data Bank, can be used to identify the flexibility of atoms, side chains, or even whole regions, and includes a discussion of limitations and possible pitfalls when using B-Factors.
Journal ArticleDOI

Protein stability engineering insights revealed by domain-wide comprehensive mutagenesis

TL;DR: An automated method to generate thermodynamic stability data for nearly every single mutant in a small 56-residue protein is developed and reveals that most single mutants have a neutral effect on stability, mutational sensitivity is largely governed by residue burial, and unexpectedly, hydrophobics are the best tolerated amino acid type.
Journal ArticleDOI

Evolutionary dynamics of SARS-CoV-2 nucleocapsid protein and its consequences.

TL;DR: Continuous monitoring is required for tracing the ongoing evolution of the SARS‐CoV‐2 N protein in prophylactic and diagnostic interventions and observing the possible consequence of high‐frequency mutations and deletions on the tertiary structure of the N protein.
Journal ArticleDOI

Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotein stability and receptor-binding affinity

TL;DR: In this paper, the authors used computational saturation mutagenesis approaches, including structure-based energy calculations and sequence-based pathogenicity predictions, to quantify the systemic effects of missense mutations on SARS-CoV-2 S protein structure and function.
Journal ArticleDOI

Computational Design of Stable and Soluble Biocatalysts

TL;DR: This work designs optimized protein sequences that maximize stability, solubility, and activity over a wide range of temperatures and pH values in buffers of different composition and in the presence of organic cosolvents.
References
More filters
Journal ArticleDOI

The FoldX web server: an online force field

TL;DR: The core functionality of FoldX, namely the calculation of the free energy of a macromolecule based on its high-resolution 3D structure, is now publicly available through a web server at FoldX.
Journal ArticleDOI

Enzyme immobilisation in biocatalysis : Why, what and how

TL;DR: An overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented and emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).
Journal ArticleDOI

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

TL;DR: This review concentrates on the remarkable thermostability of hyperthermophilic enzymes, and describes the biochemical and molecular properties of these enzymes, which are typically thermostable and optimally active at high temperatures.
Journal ArticleDOI

Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.

TL;DR: The present energy function uses a minimum of computational resources and can therefore easily be used in protein design algorithms, and in the field of protein structure and folding pathways prediction where one requires a fast and accurate energy function.
Related Papers (5)