Premium
The use of differential scanning calorimetry (DSC) to determine the correctness of folding of cloned proteins
Author(s) -
Brewer John M.
Publication year - 1999
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1999.tb00909.x
Subject(s) - differential scanning calorimetry , folding (dsp implementation) , denaturation (fissile materials) , protein folding , calorimetry , chemistry , mutant , biophysics , crystallography , biochemistry , computational biology , biology , gene , physics , thermodynamics , nuclear chemistry , electrical engineering , engineering
The advantages and limitations of use of the differential scanning calorimetry technique to determine whether cloned and expressed mutant proteins are folded correctly are explained and discussed. Examination of stabilization of these proteins to thermal denaturation by specific ligand binding can provide the required information.