Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift

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

Volumn 105, Issue 36, 2008, Pages 13362-13366

  Barstow, Buz ^a   Ando, Nozomi ^a   Kim, Chae Un ^b   Gruner, Sol M ^a,b  

^a Cornell University   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

Fluorescence; High pressure x ray crystallography; Protein engineering; Protein structure function; Yellow fluorescent protein

Indexed keywords

CITRINE; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BIOENGINEERING; CHROMATOPHORE; COOLING; CORRELATION ANALYSIS; FLUORESCENCE; HYDROSTATIC PRESSURE; MODEL; PREDICTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SPECTRUM; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; LUMINESCENT PROTEINS; MODELS, MOLECULAR; PRESSURE; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; WATER;

EID: 51649104603     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0802252105     Document Type: Article

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