Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin.

Abstract

Study holds ProTherm entries: 7360, 7361, 7362, 7363, 7364 Extra Details: absorbancy measurement; free energy of denaturation;,GdnHCl binding site; binding constant

Submission Details

ID: 69NGfptK

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:33 p.m.

Version: 1

Publication Details
Pace CN;Vanderburg KE,Biochemistry (1979) Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin. PMID:570408
Additional Information

Study Summary

Number of data points 5
Proteins Myoglobin ; Myoglobin
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: dG_H2O pH:3.2 ; Experimental Assay: dG_H2O pH:6.6 ; Experimental Assay: dG_H2O pH:4.3 ; Experimental Assay: dG_H2O pH:2.9 ; Experimental Assay: dG_H2O pH:6.0
Libraries Mutations for sequence GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG

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
5YCI 2017-09-07T00:00:00+0000 1.97 Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly)
5YCJ 2017-09-07T00:00:00+0000 1.58 Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly) imidazole-ligand
1M6C 1998-08-12T00:00:00+0000 1.9 V68N MYOGLOBIN WITH CO
1M6M 1998-08-13T00:00:00+0000 1.8 V68N MET MYOGLOBIN
1MDN 1998-08-12T00:00:00+0000 1.98 WILD TYPE MYOGLOBIN WITH CO
1MNH 1995-01-11T00:00:00+0000 2.3 INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1MNI 1995-01-11T00:00:00+0000 2.07 ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT
1MNJ 1995-01-11T00:00:00+0000 2.2 INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1MNK 1995-01-11T00:00:00+0000 2.2 INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1MNO 1998-08-13T00:00:00+0000 1.95 V68N MYOGLOBIN OXY FORM

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
90.3 Myoglobin P02163 MYG_ROUAE
90.9 Myoglobin P11343 MYG_LUTLU
90.3 Myoglobin P02165 MYG_TUPGL
90.3 Myoglobin P02167 MYG_NYCCO
90.3 Myoglobin Q0KIY0 MYG_MESST
90.3 Myoglobin P02183 MYG_MESCA
90.8 Myoglobin P02177 MYG_ESCRO
90.8 Myoglobin Q0KIY2 MYG_BALED
90.8 Myoglobin Q0KIY1 MYG_BALBO
90.9 Myoglobin P02189 MYG_PIG
90.9 Myoglobin P02166 MYG_PERPO
92.2 Myoglobin P02169 MYG_LEPMU
91.6 Myoglobin P02181 MYG_INIGE
100.0 Myoglobin P68082 MYG_HORSE
100.0 Myoglobin P68083 MYG_EQUBU
90.1 Myoglobin P02178 MYG_MEGNO