Spectral studies on the denaturation of myoglobin.


Abstract

Study holds ProTherm entries: 10124, 10125 Extra Details: spectral properties; chromophores; structual stability

Submission Details

ID: 8jwm55MZ3

Submitter: Connie Wang

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

Version: 1

Publication Details
Schechter AN;Epstein CJ,J. Mol. Biol. (1968) Spectral studies on the denaturation of myoglobin. PMID:5673697
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
6BMG 2017-11-14T00:00:00+0000 1.88 Structure of Recombinant Dwarf Sperm Whale Myoglobin (Oxy)
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

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
90.3 Myoglobin P02180 MYG_BALPH
90.8 Myoglobin P68278 MYG_PHOPH
90.8 Myoglobin P68277 MYG_PHODA
90.8 Myoglobin P68279 MYG_TURTR
90.8 Myoglobin P68276 MYG_DELDE
90.8 Myoglobin Q0KIY7 MYG1_STEAT
91.4 Myoglobin P02173 MYG_ORCOR
90.9 Myoglobin P02179 MYG_BALAC
92.1 Myoglobin P02174 MYG_GLOME
91.6 Myoglobin P02181 MYG_INIGE
91.4 Myoglobin Q0KIY3 MYG_PENEL
92.2 Myoglobin P02178 MYG_MEGNO
92.9 Myoglobin P02177 MYG_ESCRO
92.9 Myoglobin Q0KIY2 MYG_BALED
92.9 Myoglobin Q0KIY1 MYG_BALBO
96.8 Myoglobin P02184 MYG_KOGSI
96.8 Myoglobin Q0KIY5 MYG_KOGBR
100.0 Myoglobin P02185 MYG_PHYMC
90.1 Myoglobin P02182 MYG_ZIPCA
90.3 Myoglobin Q0KIY0 MYG_MESST
90.3 Myoglobin P02183 MYG_MESCA
90.3 Myoglobin P02163 MYG_ROUAE
90.9 Myoglobin P11343 MYG_LUTLU
90.3 Myoglobin P02165 MYG_TUPGL
90.3 Myoglobin P02167 MYG_NYCCO
90.9 Myoglobin P02189 MYG_PIG
90.9 Myoglobin P02166 MYG_PERPO
92.2 Myoglobin P02169 MYG_LEPMU
100.0 Myoglobin P68082 MYG_HORSE
100.0 Myoglobin P68083 MYG_EQUBU