Reply to Breuker et al.: How laser electrospray mass spectrometry (LEMS) measures condensed phase protein structure, not vacuum structure

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

Volumn 109, Issue 5, 2012, Pages

  Brady, John J ^a   Judge, Elizabeth J ^b   Levis, Robert J ^a  

^a Temple University   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; PROTEIN; SOLVENT;

ELECTROSPRAY; ELECTROSPRAY MASS SPECTROMETRY; FEMTOSECOND LASER; LASER ELECTROSPRAY MASS SPECTROMETRY; LETTER; PH; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SOLVATION; VACUUM; VAPORIZATION;

EID: 84857135276     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1116021109     Document Type: Letter

References (3)

1. Brady JJ, Judge EJ, Levis RJ (2011) Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure. Proc Natl Acad Sci USA 108:12217-12222.
2. Breuker K, Skinner OS, McLafferty FW (2012) Femtosecond laser vaporization that preserves protein-folded structure: An unproven idea. Proc Natl Acad Sci USA 109: E206.
3. Clemmer DE, Hudgins RR, Jarrold MF (1995) Naked protein conformations: Cytochrome c in the gas phase. J Am Chem Soc 117:10141-10142.