Effects of salts of alkali earth metals and calcium chloride on the stability of cytochrome c and myoglobin.


This study suggests a procedure by which binding of denaturants could be detected without any additional information other than that provided in the denaturation profiles of proteins. Two predominantly alpha-proteins, namely ferricytochrome c and metmyoglobin were denatured by guanidine hydrochloride (GdnHCl) in the presence of low fixed concentrations of salts at 25 degrees C and transition between native and denatured states was followed by absorbance measurements in the visible region (500-350 nm). The raw data were converted into transition curves from which Cm, the midpoint of GdnHCl-induced transition, and deltaGapp, the free energy changes on denaturation, were calculated assuming a two-state mechanism, and values of deltaGapp at zero concentration of the denaturant were estimated. It has been observed (1) that chlorides of Na, K, Cs, and Rb do not affect the native conformation of proteins, (2) that GdnHCl-induced denaturations of proteins in presence and absence of sodium bromide, sodium perchlorate and salts of lithium and calcium are reversible, (3) that optical properties of the GdnHCl-denatured state of proteins remain unchanged in presence of the second denaturant, (4) Cm decreases with an increase in the denaturant concentration, and (5) that except for GdnHCl there exist one or more binding sites on the native proteins for the denaturants. Study holds ProTherm entries: 10028, 10029 Extra Details: binding of denaturants;free changes on denaturation;,two-state mechanism;binding sites

Submission Details

ID: f3iFd2QK3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:39 p.m.

Version: 1

Publication Details
Ahmad Z;Yadav S;Ahmad F;Khan NZ,Biochim. Biophys. Acta (1996) Effects of salts of alkali earth metals and calcium chloride on the stability of cytochrome c and myoglobin. PMID:8639715
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 UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Cytochrome c P00004 CYC_HORSE
99.0 Cytochrome c P68097 CYC_EQUAS
99.0 Cytochrome c P68096 CYC_EQUBU
97.1 Cytochrome c P62894 CYC_BOVIN
97.1 Cytochrome c P62895 CYC_PIG
97.1 Cytochrome c P62896 CYC_SHEEP
94.3 Cytochrome c P00007 CYC_HIPAM
95.2 Cytochrome c P68099 CYC_CAMDR
95.2 Cytochrome c P68100 CYC_ESCRO
95.2 Cytochrome c P68098 CYC_LAMGU
94.3 Cytochrome c P62897 CYC_MOUSE
94.3 Cytochrome c P00008 CYC_RABIT
94.3 Cytochrome c P62898 CYC_RAT
94.3 Cytochrome c P00011 CYC_CANLF
93.3 Cytochrome c P00014 CYC_MACGI
93.3 Cytochrome c P00013 CYC_MINSC
93.3 Cytochrome c Q52V09 CYC_CEPBA
93.3 Cytochrome c P00012 CYC_MIRLE
90.5 Cytochrome c Q52V10 CYC_SAISC
92.3 Cytochrome c P81280 CYC_ALLMI
92.2 Cytochrome c P00020 CYC_ANAPL
91.3 Cytochrome c P00021 CYC_COLLI
90.3 Cytochrome c B4USV4 CYC_OTOGA
100.0 Myoglobin P68083 MYG_EQUBU
100.0 Myoglobin P68082 MYG_HORSE
91.6 Myoglobin P02181 MYG_INIGE
92.2 Myoglobin P02169 MYG_LEPMU
90.9 Myoglobin P02166 MYG_PERPO
90.9 Myoglobin P02189 MYG_PIG
90.8 Myoglobin Q0KIY1 MYG_BALBO
90.8 Myoglobin Q0KIY2 MYG_BALED
90.8 Myoglobin P02177 MYG_ESCRO
90.3 Myoglobin P02183 MYG_MESCA
90.3 Myoglobin Q0KIY0 MYG_MESST
90.3 Myoglobin P02167 MYG_NYCCO
90.3 Myoglobin P02165 MYG_TUPGL
90.9 Myoglobin P11343 MYG_LUTLU
90.3 Myoglobin P02163 MYG_ROUAE
90.1 Myoglobin P02178 MYG_MEGNO