TY  - JOUR
AU  - Rahban, Mahdie
AU  - Zolghadri, Samaneh
AU  - Salehi, Najmeh
AU  - Ahmad, Faizan
AU  - Haertlé, Thomas
AU  - Rezaie Ghaleh, Nasrollah
AU  - Sawyer, Lindsay
AU  - Saboury, Ali Akbar
TI  - Thermal stability enhancement: Fundamental concepts of protein engineering strategies to manipulate the flexible structure
JO  - International journal of biological macromolecules
VL  - 214
SN  - 0141-8130
CY  - New York, NY [u.a.]
PB  - Elsevier
M1  - FZJ-2022-05906
SP  - 642 - 654
PY  - 2022
N1  - Kein Post-Print vorhanden
AB  - Increasing the temperature by just a few degrees may lead to structural perturbation or unfolding of the protein and consequent loss of function. The concepts of flexibility and rigidity are fundamental for understanding the relationships between function, structure and stability. Protein unfolding can often be triggered by thermal fluctuations with flexible residues usually on the protein surface. Therefore, identification and knowledge of the effect of modification to flexible regions in protein structures are required for efficient protein engineering and the rational design of thermally stable proteins. The most flexible regions in protein are loops, hence their rigidification is one of the effective strategies for increasing thermal stability. Directed evolution or rational design by computational prediction can also lead to the generation of thermally stable proteins. Computational protein design has been improved significantly in recent years and has successfully produced de novo stable backbone structures with optimized sequences and functions. This review discusses intramolecular and intermolecular interactions that determine the protein structure, and the strategies utilized in the mutagenesis of mesophilic proteins to stabilize and improve the functional characteristics of biocatalysts by describing efficient techniques and strategies to rigidify flexible loops at appropriate positions in the structure of the protein.
LB  - PUB:(DE-HGF)16
C6  - 35772638
UR  - <Go to ISI:>//WOS:000861847600003
DO  - DOI:10.1016/j.ijbiomac.2022.06.154
UR  - https://juser.fz-juelich.de/record/916060
ER  -