The role of tryptophan residues in the stability of proteins was studied by ozone oxidation, which causes a small change in the tryptophan side chain. Trp 187 of the constant fragment of a type lambda immunoglobulin light chain, Trp 59 of ribonuclease T1, and Trp 62 of hen egg white lysozyme were oxidized specifically by ozone to N'-formylkynurenine or kynurenine. Judging from their circular dichroic and fluorescence spectra, these modified proteins were found to be the same as those of the respective intact proteins. However, even the slight modification of a single tryptophan residue produced a large decrease in the stability of these proteins to guanidine hydrochloride and heat. The smaller the extent of exposure of the tryptophan residue, the greater the effect of the modification on the stability. The formal kinetic mechanism of unfolding and refolding by guanidine hydrochloride of the CL fragment was not altered by tryptophan oxidation, but the rate constants for unfolding and refolding changed. The thermal unfolding transitions were analyzed to obtain the thermodynamic parameters. The enthalpy and entropy changes for the modified proteins were larger than the respective values for the intact proteins. Study holds ProTherm entries: 3670, 3671, 3672 Extra Details: tryptophan; ozone oxidation; kinetic mechanism;,thermodynamic parameters
ID: v3NpVwMu3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:22 p.m.
Version: 1
Number of data points | 3 |
Proteins | Lysozyme C ; Lysozyme C |
Unique complexes | 1 |
Assays/Quantities/Protocols | Experimental Assay: Tm |
Libraries | Mutations for sequence KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL |
Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Structure ID | Release Date | Resolution | Structure Title |
---|---|---|---|
2IHL | 1993-06-29T00:00:00+0000 | 1.4 | LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL) |
1FBI | 1995-01-19T00:00:00+0000 | 3.0 | CRYSTAL STRUCTURE OF A CROSS-REACTION COMPLEX BETWEEN FAB F9.13.7 AND GUINEA-FOWL LYSOZYME |
1GHL | 1993-05-04T00:00:00+0000 | 2.1 | THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES |
1HHL | 1993-05-04T00:00:00+0000 | 1.9 | THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES |
1JHL | 1993-05-04T00:00:00+0000 | 2.4 | THREE-DIMENSIONAL STRUCTURE OF A HETEROCLITIC ANTIGEN-ANTIBODY CROSS-REACTION COMPLEX |
1BQL | 1995-02-03T00:00:00+0000 | 2.6 | STRUCTURE OF AN ANTI-HEL FAB FRAGMENT COMPLEXED WITH BOBWHITE QUAIL LYSOZYME |
1DKJ | 1996-01-10T00:00:00+0000 | 2.0 | BOBWHITE QUAIL LYSOZYME |
1DKK | 1996-01-10T00:00:00+0000 | 1.9 | BOBWHITE QUAIL LYSOZYME WITH NITRATE |
135L | 1993-06-10T00:00:00+0000 | 1.3 | X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION |
1DZB | 2000-02-23T00:00:00+0000 | 2.0 | Crystal structure of phage library-derived single-chain Fv fragment 1F9 in complex with turkey egg-white lysozyme |
Percent Identity | Matching Chains | Protein | Accession | Entry Name |
---|---|---|---|---|
100.0 | Lysozyme C | P00698 | LYSC_CHICK | |
96.9 | Lysozyme C | P00700 | LYSC_COLVI | |
96.9 | Lysozyme C | P00699 | LYSC_CALCC | |
96.9 | Lysozyme C | Q7LZQ0 | LYSC_CATWA | |
96.9 | Lysozyme C | Q7LZP9 | LYSC_LOPIM | |
96.1 | Lysozyme C | Q7LZI3 | LYSC_TRASA | |
95.3 | Lysozyme C | P00701 | LYSC_COTJA | |
96.1 | Lysozyme C | P19849 | LYSC_PAVCR | |
95.3 | Lysozyme C | P22910 | LYSC_CHRAM | |
95.3 | Lysozyme C | Q7LZT2 | LYSC_TRATE | |
95.2 | Lysozyme C | P00703 | LYSC_MELGA | |
92.2 | Lysozyme C | P00704 | LYSC_NUMME | |
93.0 | Lysozyme C | P24364 | LYSC_LOPLE | |
94.6 | Lysozyme C | P24533 | LYSC_SYRRE | |
93.2 | Lysozyme C | P00702 | LYSC_PHACO | |
93.0 | Lysozyme C | P81711 | LYSC_SYRSO | |
92.3 | Lysozyme C | P49663 | LYSC_PHAVE |