The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability.

Abstract

The M32L substitution mutation of staphylococcal nuclease was made to test the theoretical prediction by Yamaotsu, Moriguchi and Hirono that it would be approximately 1.6 kcal/mol more stable than the wild-type protein. Instead M32L and the closely related M32I mutant were 0.8 and 0.6 kcal/mol less stable than the wild-type protein, respectively. The theoretical treatment had successfully predicted the stability effects of other mutations in staphylococcal nuclease. The discrepancy found here may be due to a general problem of the theoretical treatment, such as inadequate molecular dynamics simulation time, or possibly due to more specific difficulty in assessing the strength of the sulfur-aromatic interaction that is present in the wild-type. Study holds ProTherm entries: 7781, 7782, 7783, 7784, 7785, 7786 Extra Details: protein folding; denaturation;,sulfur-aromatic interactions; mutation

Submission Details

ID: vCMLPYcB4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Spencer DS;Stites WE,J. Mol. Biol. (1996) The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability. PMID:8648619
Additional Information

Study Summary

Number of data points 20
Proteins Thermonuclease ; Thermonuclease
Unique complexes 3
Assays/Quantities/Protocols Experimental Assay: Cm ; Experimental Assay: Tm ; Experimental Assay: dHvH ; Experimental Assay: Cm temp:20.0 C ; Experimental Assay: m ; Experimental Assay: dG_H2O ; Derived Quantity: dTm ; Derived Quantity: ddG_H2O
Libraries Mutations for sequence ATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ

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 UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Thermonuclease P00644 NUC_STAAU
99.3 Thermonuclease Q5HHM4 NUC_STAAC
99.1 Thermonuclease Q99VJ0 NUC_STAAM
99.1 Thermonuclease Q7A6P2 NUC_STAAN
99.3 Thermonuclease Q6GB41 NUC_STAAS
99.3 Thermonuclease Q8NXI6 NUC_STAAW
99.3 Thermonuclease Q6GIK1 NUC_STAAR