Abstract
How Site‐Directed Mutagenesis Alters the Solubility and Stability of RNase Sa
The FASEB journal, Vol.20(4), pp.A501-A501
03/2006
DOI: 10.1096/fasebj.20.4.A501
Abstract
The study of protein solubility has been a recurring research topic in the field of biochemistry and medicine for the last several years. Protein solubility research has allowed insight into the characteristics of human diseases including Alzheimer’s and Type II diabetes mellitus. The goals and aims of this experiment were to determine how alterations in the amino acid sequence of Ribonuclease (RNase) Sa affected the solubility of the protein. Additionally, double mutants were constructed to determine if the mutations have an additive effect. Recombinant proteins were synthesized using Escherichia coli and mutations were made to specific amino acids to obtain substantial alterations in the solubility. The data was used with accessible surface area calculations to rationalize the effects of the mutations on the solubility. The thermodynamic stability of these variants was also measured and compared to wild type. Solubility results suggest serine and threonine contribute much more favorably than asparagine. Therefore, future mutations will be made to Thr76 in order to create an amino acid solubility scale. Stability of the double mutants was additive and the overall stability of RNase Sa was not altered for the single or double mutants.
Funding for this research was from grant DBI‐013924 from the National Science Foundation (NSF).
Details
- Title: Subtitle
- How Site‐Directed Mutagenesis Alters the Solubility and Stability of RNase Sa
- Creators
- Katherine Michelle Schmalzer - Texas State UniversitySaul Trevino - Texas A&M UniversityNick Pace - Texas A&M UniversityJ. Martin Scholtz - Texas A&M University
- Resource Type
- Abstract
- Publication Details
- The FASEB journal, Vol.20(4), pp.A501-A501
- Publisher
- Federation of American Societies for Experimental Biology
- DOI
- 10.1096/fasebj.20.4.A501
- ISSN
- 0892-6638
- eISSN
- 1530-6860
- Number of pages
- 1
- Grant note
- National Science Foundation (NSF) (DBI‐013924)
- Language
- English
- Date published
- 03/2006
- Academic Unit
- Chemistry; Research Administration; Biochemistry and Molecular Biology; Pharmaceutical Sciences and Experimental Therapeutics
- Record Identifier
- 9984293416902771
Metrics
21 Record Views