Faculty Opinions recommendation of Contribution of surface salt bridges to protein stability: guidelines for protein engineering.

2003 ◽  
Author(s):  
Gideon Schreiber
Keyword(s):  
Protein Engineering ◽  
Protein Stability ◽  
Salt Bridges

Contribution of Surface Salt Bridges to Protein Stability: Guidelines for Protein Engineering

2003 ◽  
Vol 327 (5) ◽  
pp. 1135-1148 ◽  
Author(s):  
George I. Makhatadze ◽  
Vakhtang V. Loladze ◽  
Dmitri N. Ermolenko ◽  
XiaoFen Chen ◽  
Susan T. Thomas
Keyword(s):  
Protein Engineering ◽  
Protein Stability ◽  
Salt Bridges

scholarly journals Extension Protein Engineering Improves Protein Stability and Binding

2019 ◽  
Vol 116 (3) ◽  
pp. 59a
Author(s):  
Matthew J. Dominguez ◽  
Zoey L. Sharp ◽  
Valeria Jaramillo Martinez ◽  
Benjamin J. Lantz ◽  
Elliott J. Stollar
Keyword(s):  
Protein Engineering ◽  
Protein Stability

scholarly journals The Role of Electrostatic Interactions on Klentaq1 Insight for Domain Separation

2012 ◽  
Vol 6 ◽  
pp. BBI.S9390 ◽  
Author(s):  
Santi Nurbaiti ◽  
Muhamad A. Martoprawiro ◽  
Akhmaloka ◽  
Rukman Hertadi
Keyword(s):  
Protein Stability ◽  
Electrostatic Interactions ◽  
Thermal Adaptation ◽  
Atomic Level ◽  
Salt Bridges ◽  
Wild Type ◽  
Interdomain Interactions ◽  
The Relationship ◽  
Domain Separation

We investigated the relationship between the thermostability of Klentaq1 and factors stabilizing interdomain interactions. When thermal adaptation of Klentaq1 was analyzed at the atomic level, the protein was stable at 300 and 350 K. It gradually unfolded at 373 K and almost spontaneously unfolded at 400 K. Domain separation was induced by disrupting electrostatic interactions in two salt bridges formed by Lys354-Glu445 and Asp371-Arg435 on the interface domain. The role of these interactions in protein stability was evaluated by comparing free energy solvation (ΔΔGsolv) between wild type and mutants. Substitution of Asp371 by Glu or Asn, and also Glu445 by Asn resulted in a positive value of ΔΔGsolv, suggesting that mutations destabilized the protein structure. Nevertheless, substitution of Glu445 by Asp gave a negative value to ΔΔGsolv reflecting increasing protein stability. Our results demonstrate that interactions at the interface domains of Klentaq1 are essential factors correlated with the Klentaq1 thermostability.

Sign in / Sign up

Export Citation Format

Share Document