Table 1.

Comparison of associability with GRP78/BiP, in silico-predicted thermal stability and other properties among wild-type and I56-mutated human lysozyme.

Lysozyme	Secretion to medium	Pelleting	Association to GRP78/BiP	Thermal stability	Property of amino acid 56
Wild type 56I	+++	±	-	+++	Hydrophobic
I56L*	+++	-	-	++	=
I56V*	+++	-	±	+	=
I56M*	+++	-	±	+	=
I56A	++	+++	+++	- - -	=
I56G	-	+++	+++	- - - -	=
I56F	++	+++	+++	+	=
I56W	-	+++	+++	- -	=
I56T**	++	+++	+++	- - -	Hydrophilic
I56E	-	+++	+++	- - -	=
I56R	-	+++	+++	- -	=
I56S	-	+++	+++	- - -	=
I56Y	-	+++	+++	++	=

I56L etc., lysozyme mutants denoted by intrinsic and substituted amino acids framing the residue number; *, those with wild-type like properties; **, that belongs to the so-called amyloidogenic variants. = is used as ditto mark. Columns 2, 3 and 4 are from the first, fourth and third panels, respectively, of Fig. 8A. Relative thermal stability was predicted by computer simulation (see text). The score shows rough degree, where +, intensive or stable; ±, subtle; -, negative or unstable. Also unused I56X mutants were simulated for the stability. When X was hydrophobic amino acid, most of the scores were ++ or +, and when X was hydrophilic one, most of the scores were - - - or - -. I67Y and I56C gave the score of ++.