Protein stability and electrostatic interactions between solvent exposed charged side chains.


Abstract

To investigate the contribution to protein stability of electrostatic interactions between charged surface residues, we have studied the effect of substituting three negatively charged solvent exposed residues with their side-chain amide analogs in bovine calbindin D9k--a small (Mr 8,500) globular protein of the calmodulin superfamily. The free energy of urea-induced unfolding for the wild-type and seven mutant proteins has been measured. The mutant proteins have increased stability towards unfolding relative to the wild-type. The experimental results correlate reasonably well with theoretically calculated relative free energies of unfolding and show that electrostatic interactions between charges on the surface of a protein can have significant effects on protein stability. Study holds ProTherm entries: 2512, 2513, 2514, 2515, 2516, 2517, 2518, 2519 Extra Details: additive : EDTA(0.3 mM),ddG was measured in the presence of 5M urea urea induced unfolding; increased stability; calbindin D9k;,site-directed mutagenesis

Submission Details

ID: 9rAd7AFM

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:19 p.m.

Version: 1

Publication Details
Akke M;Forsén S,Proteins (1990) Protein stability and electrostatic interactions between solvent exposed charged side chains. PMID:2217161
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
2BCB 1993-10-31 HIGH-RESOLUTION SOLUTION STRUCTURE OF CALCIUM-LOADED CALBINDIN D9K
1B1G 1998-11-25 SOLVATED REFINEMENT OF CA-LOADED CALBINDIN D9K
1BOC 1993-10-31 THE SOLUTION STRUCTURES OF MUTANT CALBINDIN D9K'S, AS DETERMINED BY NMR, SHOW THAT THE CALCIUM BINDING SITE CAN ADOPT DIFFERENT FOLDS
1KSM 2002-01-23 AVERAGE NMR SOLUTION STRUCTURE OF CA LN CALBINDIN D9K
1KCY 2001-11-21 NMR solution structure of apo calbindin D9k (F36G + P43M mutant)
1N65 2003-11-18 FAMILY OF NMR SOLUTION STRUCTURES OF CA CE CALBINDIN D9K IN DENATURATING CONDITIONS
1BOD 1993-10-31 THE SOLUTION STRUCTURES OF MUTANT CALBINDIN D9K'S, AS DETERMINED BY NMR, SHOW THAT THE CALCIUM BINDING SITE CAN ADOPT DIFFERENT FOLDS
1RT0 2005-07-26 12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordinating Zn(II)
1KQV 2002-01-16 Family of NMR Solution Structures of Ca Ln Calbindin D9K
2BCA 1993-10-31 HIGH-RESOLUTION SOLUTION STRUCTURE OF CALCIUM-LOADED CALBINDIN D9K
2MAZ 2013-08-07 Backbone 1H, 13C, and 15N Chemical Shift Assignments for Bovine Apo Calbindin
1D1O 2000-03-08 COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K
1CLB 1995-04-20 Determination of the solution structure of apo calbindin D9K by nmr spectroscopy
1CDN 1995-11-14 Solution structure of (CD2+)1-calbindin D9K reveals details of the stepwise structural changes along the apo--> (CA2+)II1--> (CA2+)I,II2 binding pathway
1QX2 2004-05-25 1.44 X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution
1IG5 2001-04-25 1.5 BOVINE CALBINDIN D9K BINDING MG2+
4ICB 1993-10-31 1.6 PROLINE CIS-TRANS ISOMERS IN CALBINDIN D9K OBSERVED BY X-RAY CRYSTALLOGRAPHY
1HT9 2001-05-09 1.76 DOMAIN SWAPPING EF-HANDS
1IGV 2001-04-25 1.85 BOVINE CALBINDIN D9K BINDING MN2+
3ICB 1986-10-24 2.3 THE REFINED STRUCTURE OF VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN FROM BOVINE INTESTINE. MOLECULAR DETAILS, ION BINDING, AND IMPLICATIONS FOR THE STRUCTURE OF OTHER CALCIUM-BINDING PROTEINS

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Protein S100-G P02633 S100G_BOVIN