Conformational free energies of myoglobins of small mammals.

Abstract

Myoglobins from three small placental mammals and one small marsupial were isolated from cardiac or skeletal muscle. The conformational free energies of these four myoglobins were estimated from guanidinium chloride unfolding data at pH 8 and 25 degrees. The myoglobins from rat and rabbit are more stable than that of the most stable myoglobin previously studied, that of the sperm whale. In addition, these two myoglobins unfold with greater cooperativity than previously characterized myoglobins. The data obtained herein demonstrate unequivocally for the first time that the stability of homeotherm myoglobins correlates with neither the size of the organism nor its metabolic rate. Study holds ProTherm entries: 10112, 10113, 10114, 10115 Extra Details: denaturation; guanidinium chloride; mammals;,myoglobin

Submission Details

ID: qf2FpHPv

Submitter: Connie Wang

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

Version: 1

Publication Details
Kelly L;Simmons JH;Heck T;Holladay LA,Int. J. Pept. Protein Res. (1988) Conformational free energies of myoglobins of small mammals. PMID:3372133
Additional Information

Study Summary

Number of data points 4
Proteins Myoglobin ; Myoglobin ; Myoglobin
Unique complexes 3
Assays/Quantities/Protocols Experimental Assay: dG
Libraries Mutations for sequence MGLSDGEWQLVLNVWGKVEGDLAGHGQEVLIKLFKNHPETLEKFDKFKHLKSEDEMKGSEDLKKHGNTVLTALGGILKKKGQHAAEIQPLAQSHATKHKIPIKYLEFISEAIIQVLQSKHPGDFGADAQGAMSKALELFRNDIAAKYKELGFQG ; Mutations for sequence MGLSDGEWQLVLNAWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGNILKKKGNHEAELKPLAQSHATKHKISVQFLEFISEAIIQVIQSKHPGDFGGDAQAAMGKALELFRNDMAAKYKELGFQG ; Mutations for sequence MGLSDAEWQLVLNVWGKVEADLAGHGQEVLIRLFHTHPETLEKFDKFKHLKSEDEMKASEDLKKHGNTVLTALGAILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISEAIIHVLHSKHPGDFGADAQAAMSKALELFRNDIAAQYKELGFQG

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
5YCJ 2018-09-19 1.58 Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly) imidazole-ligand
3RGK 2011-04-27 1.65 Crystal Structure of Human Myoglobin Mutant K45R
1MWC 1998-08-19 1.7 WILD TYPE MYOGLOBIN WITH CO
1MYG 1994-01-31 1.75 HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
1M6M 1998-08-19 1.8 V68N MET MYOGLOBIN
1MWD 1998-08-19 1.8 WILD TYPE DEOXY MYOGLOBIN
1MYJ 1994-01-31 1.9 DISTAL POLARITY IN LIGAND BINDING TO MYOGLOBIN: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A THREONINE68(E11) MUTANT
1MYH 1994-01-31 1.9 HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
1M6C 1998-08-19 1.9 V68N MYOGLOBIN WITH CO
1MNO 1998-08-19 1.95 V68N MYOGLOBIN OXY FORM
5YCI 2018-09-19 1.97 Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly)
1MDN 1998-09-30 1.98 WILD TYPE MYOGLOBIN WITH CO
1MYI 1994-01-31 2.0 HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
1MNI 1995-04-20 2.07 ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT
1YCB 1994-01-31 2.1 DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN: DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 (E11) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY
1MNJ 1995-04-20 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 1995-04-20 2.2 INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1MNH 1995-05-08 2.3 INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1PMB 1990-01-15 2.5 THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT
1YCA 1994-01-31 2.9 DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN: DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 (E11) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Myoglobin P02193 MYG_DIDVI
92.2 Myoglobin P02163 MYG_ROUAE
90.9 Myoglobin P68086 MYG_ERYPA
90.9 Myoglobin P68084 MYG_PAPAN
90.9 Myoglobin P68085 MYG_SEMEN
90.3 Myoglobin P02144 MYG_HUMAN
90.9 Myoglobin P20856 MYG_CTEGU
90.3 Myoglobin P02150 MYG_MACFA
92.9 Myoglobin P02189 MYG_PIG
100.0 Myoglobin P02170 MYG_RABIT
92.9 Myoglobin P02165 MYG_TUPGL
90.3 Myoglobin P02181 MYG_INIGE
94.2 Myoglobin P11343 MYG_LUTLU
90.9 Myoglobin P02166 MYG_PERPO
90.3 Myoglobin P02145 MYG_PANTR
100.0 Myoglobin P04248 MYG_SPAEH
93.5 Myoglobin P02171 MYG_OCHPR
90.3 Myoglobin P02167 MYG_NYCCO
92.9 Myoglobin P04249 MYG_PROGU
92.2 Myoglobin Q6PL31 MYG_OCHCU
91.6 Myoglobin C0HJQ9 MYG_HYSCR
91.6 Myoglobin P04250 MYG_LAGMA
90.3 Myoglobin P02164 MYG_ORYAF
90.3 Myoglobin P02156 MYG_ERIEU
90.3 Myoglobin P02157 MYG_MELME
90.3 Myoglobin C0HKB7 MYG_SCIVU