Reversible denaturation of the gene V protein of bacteriophage f1.


Abstract

The guanidine hydrochloride (GuHCl)-induced denaturation of the gene V protein of bacteriophage f1 has been studied, using the chemical reactivity of a cysteine residue that is buried in the folded protein and the circular dichroism (CD) at 211 and 229 nm as measures of the fraction of polypeptide chains in the folded form. It is found that this dimeric protein unfolds in a single cooperative transition from a folded dimer to two unfolded monomers. A folded, monomeric form of the gene V protein was not detected at equilibrium. The kinetics of unfolding of the gene V protein in 3 M GuHCl and the refolding in 2 M GuHCl are also consistent with a transition between a folded dimer and two unfolded monomers. The GuHCl concentration dependence of the rates of folding and unfolding suggests that the transition state for folding is near the folded conformation. Study holds ProTherm entries: 4228 Extra Details: additive : EDTA(0.001 M), chemical reactivity; cysteine; buried; dimeric protein;,cooperative transition

Submission Details

ID: ey8g9BWU

Submitter: Connie Wang

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

Version: 1

Publication Details
Liang H;Terwilliger TC,Biochemistry (1991) Reversible denaturation of the gene V protein of bacteriophage f1. PMID:2007116
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
2GVA 1995-10-15 REFINED SOLUTION STRUCTURE OF THE TYR 41--> HIS MUTANT OF THE M13 GENE V PROTEIN. A COMPARISON WITH THE CRYSTAL STRUCTURE
2GVB 1995-10-15 REFINED SOLUTION STRUCTURE OF THE TYR 41--> HIS MUTANT OF THE M13 GENE V PROTEIN. A COMPARISON WITH THE CRYSTAL STRUCTURE
1GVP 1997-09-04 1.6 GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
1GKH 1997-09-04 1.7 MUTANT K69H OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
1VQI 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH ILE 47 REPLACED BY VAL 47 (I47V)
1VQE 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)
1VQC 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY PHE 47 (V35I, I47F)
1VQH 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH ILE 47 REPLACED BY MET 47 (I47M)
1VQA 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ALA 35 AND ILE 47 REPLACED BY LEU 47 (V35A, I47L)
1VQJ 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 (V35I)
1VQB 1997-02-12 1.8 GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
1VQF 1997-02-12 1.8 GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY VAL 47 (V35I, I47V)
1VQD 1997-02-12 1.82 GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)
1VQG 1997-02-12 1.82 GENE V PROTEIN MUTANT WITH ILE 47 REPLACED BY LEU 47 (I47L)
1AE3 1997-09-04 2.0 MUTANT R82C OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
1AE2 1997-09-04 2.0 MUTANT L32R OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
1YHB 1994-06-22 2.2 CRYSTAL STRUCTURES OF Y41H AND Y41F MUTANTS OF GENE V PROTEIN FROM FF PHAGE SUGGEST POSSIBLE PROTEIN-PROTEIN INTERACTIONS IN GVP-SSDNA COMPLEX
2GN5 1986-01-21 2.3 REFINED STRUCTURE OF THE GENE 5 DNA BINDING PROTEIN FROM BACTERIOPHAGE FD
1YHA 1994-06-22 2.5 CRYSTAL STRUCTURES OF Y41H AND Y41F MUTANTS OF GENE V PROTEIN FROM FF PHAGE SUGGEST POSSIBLE PROTEIN-PROTEIN INTERACTIONS IN GVP-SSDNA COMPLEX

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 DNA-Binding protein G5P P69544 G5P_BPM13
100.0 DNA-Binding protein G5P P69542 G5P_BPFD
100.0 DNA-Binding protein G5P P69543 G5P_BPF1