The structure of Fis mutant Pro61Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
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2. The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS;Protein Science;2011-01-28
3. Thermodynamics of replacing an α-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin;Protein Science;2008-12-31
4. A truncated peptide model of the mutant P61A FIS forms a stable dimer;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2007-01
5. Common and Variable Contributions of Fis Residues to High-Affinity Binding at Different DNA Sequences;Journal of Bacteriology;2006-03-15
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