The perturbation of tryptophan fluorescence by phenylalanine to alanine mutations identifies the hydrophobic core in a subset of bacterial Ig-like domains

Biochemistry

Volumn 52, Issue 27, 2013, Pages 4589-4591

  Raman, Rajeev ^a   Ptak, Christopher P ^b   Hsieh, Ching Lin ^b   Oswald, Robert E ^b   Chang, Yung Fu ^b   Sharma, Yogendra ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

^b Department of Molecular Medicine College of Veterinary Medicine Cornell University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBICITY; PROTEINS;

ALANINE MUTATIONS; HOST PROTEINS; HOST-PARASITE INTERACTIONS; HYDROPHOBIC CORE; SPECTRAL PROPERTIES; TRYPTOPHAN FLUORESCENCE;

AMINO ACIDS;

ALANINE; FIBRONECTIN; IMMUNOGLOBULIN; PHENYLALANINE; TRYPTOPHAN;

ANISOTROPY; ARTICLE; ENZYME LINKED IMMUNOSORBENT ASSAY; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; ARTHROBACTER; CHEMICAL PHENOMENA; CHEMISTRY; FLUORESCENCE;

ALANINE; ARTHROBACTER; FLUORESCENCE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; IMMUNOGLOBULINS; PHENYLALANINE; TRYPTOPHAN;

EID: 84880055356     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400128r     Document Type: Article

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