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Dynamic light scattering study of the two‐domain structure of Humicola insolens endoglucanase V
Author(s) -
Boisset Claire,
Borsali Redouane,
Schülein Martin,
Henrissat Bernard
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01244-0
Subject(s) - trichoderma reesei , cellulase , domain (mathematical analysis) , chemistry , relaxation (psychology) , radius , physics , crystallography , cellulose , mathematics , mathematical analysis , biochemistry , biology , computer security , computer science , neuroscience
Endoglucanase V (EG V) of Humicola insolens is composed of a catalytic domain and of a cellulose‐binding domain linked by a 33 amino acid long peptide rich in Ser, Thr and Pro residues. This work describes the dynamic behavior of the two‐domain structure of EG V as revealed by quasi‐elastic light scattering experiments. For both the full‐length and the isolated catalytic domain, the autocorrelation function is essentially described by a single relaxation mode. The equivalent hydrodynamic radius of the catalytic domain was found to correspond precisely to the dimensions measured from the previously determined three‐dimensional structure. The results obtained with the full‐length protein allow a description of the two domain structure of EG V similar to that resulting from earlier studies using small angle X‐ray scattering on cellulases from Trichoderma reesei . The hydrodynamic dimensions of the entire enzyme can be approximated as an ellipsoid with dimensions of .