Solution structure of a minor and transiently formed state of a T4 lysozyme mutant

Structure of a protein intermediate The function of a protein depends critically on structural dynamics, and on the nature of the transient conformation intermediates that the molecule can adopt. These transients can be elusive and therefore hard to characterize. This paper reports the use of a comb...

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Veröffentlicht in:	Nature (London) 2011-09, Vol.477 (7362), p.111-114
Hauptverfasser:	Bouvignies, Guillaume, Vallurupalli, Pramodh, Hansen, D. Flemming, Correia, Bruno E., Lange, Oliver, Bah, Alaji, Vernon, Robert M., Dahlquist, Frederick W., Baker, David, Kay, Lewis E.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/535 631/57/2272/2273 Bacteriophage T4 - enzymology Bacteriophage T4 - genetics Biological and medical sciences Conformational dynamics in molecular biology Crystal structure Enzymes Evolution, Molecular Experiments Fundamental and applied biological sciences. Psychology Gene mutations Humanities and Social Sciences Hydrophobic and Hydrophilic Interactions letter Ligands Lysozyme Models, Molecular Molecular biophysics multidisciplinary Muramidase - chemistry Muramidase - genetics Mutation Phage T4 Physiological aspects Protein Binding Proteins Science Science (multidisciplinary) Temperature
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