Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase.

Abstract

The reversible denaturation of protein disulfide isomerase proceeds through intermediates that are stabilized by interaction with guanidine hydrochloride. At pH 7.5, the equilibrium denaturation by urea is completely reversible and the transition can be reasonably well-described by a two-state model involving only native and denatured forms. In comparison, the equilibrium denaturation by guanidine hydrochloride occurs in two distinct steps. In the presence of a low constant amount of guanidine hydrochloride (0.5-1.4 M), urea denaturation also becomes biphasic, suggesting the accumulation of an intermediate species that is stabilized by specific interaction with guanidine hydrochloride but not by high concentrations of other salts or other denaturants. Study holds ProTherm entries: 11060, 11061, 11062, 11063, 11064, 11065, 11066, 11067, 11068, 11069, 11070, 11071 Extra Details: additive : EDTA(5 mM),N->I intermediates; two-state model; specific interaction

Submission Details

ID: FG85VKoJ4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Morjana NA;McKeone BJ;Gilbert HF,Proc. Natl. Acad. Sci. U.S.A. (1993) Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. PMID:8460117
Additional Information

Study Summary

Number of data points 12
Proteins Protein disulfide-isomerase
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: dG buffers:sodium phosphate: 0.2 M ; Experimental Assay: dG buffers:sodium phosphate: 0.2 M ; Experimental Assay: dG buffers:potassium phosphate: 0.2 M ; Experimental Assay: dG buffers:potassium phosphate: 0.2 M ; Experimental Assay: dG buffers:potassium phosphate: 0.2 M
Libraries Mutations for sequence MLRRALLCLALTALFRAGAGAPDEEDHVLVLHKGNFDEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAASTLSDGAAAEALVESSEVAVIGFFKDMESDSAKQFFLAAEVIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLSNFKKAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQELPDDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDLEEDDDQKAVKDEL

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 Protein disulfide-isomerase P05307 PDIA1_BOVIN
91.2 Protein disulfide-isomerase Q8R4U2 PDIA1_CRIGR
94.1 Protein disulfide-isomerase P07237 PDIA1_HUMAN
91.0 Protein disulfide-isomerase P09103 PDIA1_MOUSE
91.0 Protein disulfide-isomerase P04785 PDIA1_RAT
93.3 Protein disulfide-isomerase Q2HWU2 PDIA1_MACFU
93.5 Protein disulfide-isomerase Q5R5B6 PDIA1_PONAB