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Conserved nucleation sites reinforce the significance of Phi value analysis in protein-folding studies
- Source :
- IUBMB Life, IUBMB Life, Wiley, 2014, 66 (7), pp.449-52. ⟨10.1002/iub.1287⟩
- Publication Year :
- 2014
- Publisher :
- HAL CCSD, 2014.
-
Abstract
- International audience; The only experimental strategy to address the structure of folding transition states, the so-called Φ value analysis, relies on the synergy between site directed mutagenesis and the measurement of reaction kinetics. Despite its importance, the Φ value analysis has been often criticized and its power to pinpoint structural information has been questioned. In this hypothesis, we demonstrate that comparing the Φ values between proteins not only allows highlighting the robustness of folding pathways but also provides per se a strong validation of the method.
- Subjects :
- Models, Molecular
MESH: Conserved Sequence
MESH: Protein Folding
Proteins
homologous proteins
MESH: Amino Acid Sequence
kinetics
protein folding
Thermodynamics
MESH: Proteins
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Amino Acid Sequence
MESH: Thermodynamics
Conserved Sequence
mutagenesis
MESH: Models, Molecular
Subjects
Details
- Language :
- English
- ISSN :
- 15216543 and 15216551
- Database :
- OpenAIRE
- Journal :
- IUBMB Life, IUBMB Life, Wiley, 2014, 66 (7), pp.449-52. ⟨10.1002/iub.1287⟩
- Accession number :
- edsair.pmid.dedup....79f5d88ff45cb611f1e7bd8260cf84e8