Use of SANS and biophysical techniques to reveal subtle conformational differences between native apo-calmodulin and its unfolded states

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1824, Issue 10, 2012, Pages 1097-1106

  Gibrat, Gabriel ^a   Assairi, Liliane ^b   Craescu, Constantin T ^b   Hui Bon Hoa, Gaston ^c   Loew, Damarys ^d   Lombard, Bérangère ^d   Blouquit, Laura ^b   Bellissent Funel, Marie Claire ^a  

^a CEA SACLAY   (France)

^b Centre Universitaire   (France)

^c INSERM   (France)

^d INSTITUT CURIE   (France)

Author keywords

Calmodulin; Circular dichroism; Fluorescence and UV absorbance; Heat denaturation; Mass spectrometry; Small angle neutron scattering

Indexed keywords

APO CALMODULIN; CALMODULIN; POLYMER; TYROSINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COOLING; DEAMINATION; FLUORESCENCE ANALYSIS; HEATING; HIGH TEMPERATURE; MASS SPECTROMETRY; NEUTRON SCATTERING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN REFOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; SEQUENCE HOMOLOGY; THERMODYNAMICS; ULTRAVIOLET SPECTROPHOTOMETRY;

BIOPHYSICS; CALMODULIN; CIRCULAR DICHROISM; NEUTRON DIFFRACTION; PROTEIN CONFORMATION; SCATTERING, SMALL ANGLE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS;

EID: 84864052560     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.06.001     Document Type: Article

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