Constant fragments with different carboxyl terminals, CL(109-211), CL(109-207), and CL-(109-200), were prepared by limited carboxypeptidase P or Y proteolysis of the constant fragment, CL-(109-214), of a type lambda immunoglobulin light chain, and their conformations and stabilities, and formation of the disulfide bond from the reduced fragments, were studied. No change in conformation or stability was observed on removal of three residues from the C-terminal end. Removal of seven or more residues from the C-terminal end destabilized the CL fragment. The rate of disulfide bond formation from reduced CL(109-207) was about 7 times faster than that for CL(109-214). These findings suggest that elongation of the polypeptide chain at least beyond the 207th residue is necessary for folding of the CL fragment into a definite conformation. Study holds ProTherm entries: 3982, 3983, 3984, 3985, 3986, 3987 Extra Details: constant fragments; conformations; disulfide bond; stability
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:23 p.m.
|Number of data points||15|
|Proteins||Immunoglobulin kappa variable 1D-33 ; Immunoglobulin kappa variable 4-1|
|Assays/Quantities/Protocols||Experimental Assay: Cm ; Experimental Assay: m ; Experimental Assay: dG_H2O ; Experimental Assay: Tm ; Experimental Assay: dHvH|
|Libraries||Mutations for sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNSKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYSFGQGTKLEIKRTVAAPSVF|