Stabilization of lysozyme by the introduction of Gly-Pro sequence.


Abstract

Three mutant lysozymes where the Asp101-Gly102 sequence of lysozyme was converted to Asp101-Pro102, Gly101-Pro102 and Pro101-Gly102 were prepared to investigate the effect of proline residues on the stabilization of proteins. The free energy changes of lysozymes for the unfolding in aqueous solution at pH 5.5 and 35 degrees C were 10.0, 10.1, 11.0 and 7.7 kcal/mol for wild type, Asp101Pro102, Gly101Pro102 and Pro101Gly102 lysozyme respectively. When the energy level in the unfolded state of wild type lysozyme was fixed at a standard level, the energy levels in the folded state of Asp101Pro102 and Pro101Gly102 lysozymes were found to be higher than that of wild type lysozyme on the basis of delta GD(H2O) and entropy losses of their polypeptide chains in the unfolded state. The presence of some strain in the folded state of these lysozymes was supported by both the calculation of conformational energy for a trans-L-prolyl residue [Schimmel, P.R. and Flory, P.J. (1968) J. Mol. Biol., 34, 105-120] and the analysis of structures of energy-minimized mutant lysozymes. Therefore, it is concluded that the formation of the Gly-Pro sequence is effective in avoiding possible strain in the folded state of a protein caused by the introduction of proline residue(s). Study holds ProTherm entries: 121, 122, 123, 2160 Extra Details: free energy change; conformational energy; lysozyme

Submission Details

ID: r9vSpt3N3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:14 p.m.

Version: 1

Publication Details
Ueda T;Tamura T;Maeda Y;Hashimoto Y;Miki T;Yamada H;Imoto T,Protein Eng. (1993) Stabilization of lysozyme by the introduction of Gly-Pro sequence. PMID:8475043
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

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

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
92.3 Lysozyme C P49663 LYSC_PHAVE
93.0 Lysozyme C P81711 LYSC_SYRSO
93.2 Lysozyme C P00702 LYSC_PHACO
94.6 Lysozyme C P24533 LYSC_SYRRE
93.0 Lysozyme C P24364 LYSC_LOPLE
92.2 Lysozyme C P00704 LYSC_NUMME
95.2 Lysozyme C P00703 LYSC_MELGA
95.3 Lysozyme C Q7LZT2 LYSC_TRATE
95.3 Lysozyme C P22910 LYSC_CHRAM
96.1 Lysozyme C P19849 LYSC_PAVCR
95.3 Lysozyme C P00701 LYSC_COTJA
96.1 Lysozyme C Q7LZI3 LYSC_TRASA
96.9 Lysozyme C Q7LZP9 LYSC_LOPIM
96.9 Lysozyme C Q7LZQ0 LYSC_CATWA
96.9 Lysozyme C P00699 LYSC_CALCC
96.9 Lysozyme C P00700 LYSC_COLVI
100.0 Lysozyme C P00698 LYSC_CHICK