Reply to Kitahara and Mulder: An ensemble view of protein stability best explains pressure effects in a T4 lysozyme cavity mutant

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 9, 2015, Pages E924-

  Wand, A Joshua ^a   Nucci, Nathaniel V ^b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b ROWAN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME;

CELL MUTANT; CRYOPROBE; CRYSTALLIZATION; ENERGY; HYPERBARISM; LETTER; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN STABILITY; REVERSE MICELLE; SOLVATION; X RAY CRYSTALLOGRAPHY; CHEMISTRY; ENTEROBACTERIA PHAGE T4; ENZYMOLOGY; PROTEIN UNFOLDING;

BACTERIOPHAGE T4; MURAMIDASE; PROTEIN UNFOLDING;

EID: 84924117582     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1424002112     Document Type: Letter

References (5)

1. 4 lysozyme due to unfolding? Proc Natl Acad Sci USA 112: E923.
2. 4 lysozyme. Proc Natl Acad Sci USA 111(38): 13846-13851.
3. Ando N, et al. (2008) Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation. Biochemistry 47(42): 11097-11109.
4. Bouvignies G, et al. (2011) Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature 477(7362): 111-114.
5. Maeno A, et al. (2015) Cavity as a source of conformational fluctuation and high-energy state: High-pressure NMR study of a cavity-enlarged mutant of T4Lysozyme. Biophys J 108(1): 133-145.