Amanote Research
Register
Sign In
Probing Denatured State Conformational Bias in a Three-Helix Bundle, UBA(2), Using a Cytochrome C Fusion Protein
doi 10.1021/acs.biochem.8b00015.s001
Full Text
Open PDF
Abstract
Available in
full text
Date
Unknown
Authors
Unknown
Publisher
American Chemical Society (ACS)
Related search
Residual Structure in the Denatured State of a Three-Helix Bundle Protein
Biophysical Journal
Biophysics
Conformational Switching at Cytochrome a During Steady-State Turnover of Cytochrome C Oxidase
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
Cytochrome C: A Multifunctional Protein Combining Conformational Rigidity With Flexibility
New Journal of Science
A Dynamic Bundle of Four Adjacent Hydrophobic Segments in the Denatured State of Staphylococcal Nuclease
Protein Science
Biochemistry
Medicine
Molecular Biology
A Novel Protein-Protein Interaction Mode Identified in Complex Structure of Cytochrome C-Cytochrome C Oxidase
Seibutsu Butsuri
Kinetoplastid Membrane Protein-11 Adopts a Four-Helix Bundle Fold in DPC Micelle
FEBS Letters
Genetics
Cell Biology
Molecular Biology
Biochemistry
Structural Biology
Biophysics
Characterization of a Mouse Somatic Cytochrome C Gene and Three Cytochrome C Pseudogenes
Nucleic Acids Research
Genetics
A Structural, Dynamic, and Thermodynamic Explanation of Thermostability in a De Novo Designed Three-Helix Bundle
Biophysical Journal
Biophysics
Basic Tilted Helix Bundle – A New Protein Fold in Human FKBP25/FKBP3 and HectD1
Biochemical and Biophysical Research Communications
Biochemistry
Cell Biology
Molecular Biology
Biophysics