Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies.


Abstract

The mutant protein I3C-C97/C54T of phage T4 lysozyme is free of sulfhydryl groups and has a genetically engineered disulfide bridge between positions 3 and 97 (Perry & Wetzel, 1986). This protein has a maximum stability at 12 degrees C in 3 M guanidinium chloride and undergoes reversible high- and low-temperature melting at 28 and -3 degrees C, respectively, in this medium. The free energy of stabilization of the protein has been studied over a range of temperature that includes both melting transitions. The stability curve fits a constant delta Cp model over the entire range, permitting an unusually complete determination of the thermodynamic parameters of the protein and demonstrating that the low-temperature unfolded form of the protein may be interpreted as an extrapolation with constant delta Cp of the high-temperature unfolded form. The free energy of unfolding is a linear function of guanidinium concentration within experimental error which permits a rough estimate of the stability of the protein at low temperatures and of the differential interaction of the unfolded protein with guanidinium chloride. These equilibrium studies provide a basis for the interpretation of the kinetic studies reported in the following paper. Study holds ProTherm entries: 3831, 3832, 3833, 3834 Extra Details: low-temperature unfolding; equilibrium studies;,stability curve; constant delta Cp model

Submission Details

ID: 2Nq7CpSt

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:22 p.m.

Version: 1

Publication Details
Chen BL;Schellman JA,Biochemistry (1989) Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. PMID:2653427
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
102L 1992-09-29T00:00:00+0000 1.74 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
103L 1992-09-29T00:00:00+0000 1.9 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
104L 1992-09-29T00:00:00+0000 2.8 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
107L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
108L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
109L 1992-12-17T00:00:00+0000 1.85 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
110L 1992-12-17T00:00:00+0000 1.7 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
111L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
112L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
113L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Endolysin P00720 ENLYS_BPT4