A comparative study of the unfolding thermodynamics of vertebrate metmyoglobins.


Abstract

Differential scanning microcalorimetry (DSC) of horse, rat, opossum, raccoon, carp, and armadillo metmyoglobins at alkaline pH gave data that fit the two-state unfolding model well. Monte Carlo studies were used to assess the impact of truncating DSC scans on the reliability of the calculated results when aggregation exotherms overlapped the unfolding endotherm at the high-temperature end of the scan. The DSC estimates for the conformational free energy at pH 8 and 298 K are compared to earlier results from isothermal acid and guanidinium chloride unfolding. Stability estimates at pH 8 for these six metmyoglobins obtained by DSC experiments do not agree with free energy estimates at pH 8 from guanidinium chloride unfolding. This is true for all three models used to extrapolate the free energy change to 0 M guanidinium chloride. Among these six myoglobins, significant variation appears in the temperature at which the myoglobin is half-unfolded, in the change in heat capacity upon unfolding, and in the change in enthalpy at 310 K. Calculations made with the hydrophobic model for protein folding [Baldwin, R.L. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 8069] suggest that a sizable variation exists for that portion of the unfolding enthalpy change assigned to forces other than the hydrophobic effect. Study holds ProTherm entries: 3713, 3714, 3715, 3716, 3717, 3718, 3719, 3720, 3721, 3722, 3723, 3724, 3725, 3726, 3727, 3728, 3729, 3730, 3731, 3732, 3733, 3734, 3735, 3736, 3737, 3738, 3739, 3740, 3741, 3742, 3743, 3744, 3745, 3746, 3747, 3748, 3749, 3750, 3751, 3752, 3753, 3754, 3755, 3756, 3757, 3758, 3759, 3760, 3761, 3762, 3763, 3764, 3765, 3766, 3767, 3768, 3769, 3770, 3771, 3772, 3773, 3774, 3775, 3776, 3777 Extra Details: two-state unfolding model; monte Carlo studies;,hydrophobic model; unfolding endotherm; sizable variation

Submission Details

ID: tcw8pnK63

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:22 p.m.

Version: 1

Publication Details
Kelly L;Holladay LA,Biochemistry (1990) A comparative study of the unfolding thermodynamics of vertebrate metmyoglobins. PMID:2378866
Additional Information

Study Summary

Number of data points 191
Proteins Myoglobin ; Myoglobin ; Myoglobin ; Myoglobin ; Myoglobin
Unique complexes 4
Assays/Quantities/Protocols Experimental Assay: dCp pH:9.56 ; Experimental Assay: dHcal pH:9.56 ; Experimental Assay: Tm pH:9.56 ; Experimental Assay: dCp pH:10.0 ; Experimental Assay: dHcal pH:10.0 ; Experimental Assay: Tm pH:10.0 ; Experimental Assay: dCp pH:10.39 ; Experimental Assay: dHcal pH:10.39 ; Experimental Assay: Tm pH:10.39 ; Experimental Assay: dCp pH:10.55 ; Experimental Assay: dHcal pH:10.55 ; Experimental Assay: Tm pH:10.55 ; Experimental Assay: dCp pH:10.66 ; Experimental Assay: dHcal pH:10.66 ; Experimental Assay: Tm pH:10.66 ; Experimental Assay: dCp pH:10.92 ; Experimental Assay: dHcal pH:10.92 ; Experimental Assay: Tm pH:10.92 ; Experimental Assay: dCp pH:11.18 ; Experimental Assay: dHcal pH:11.18 ; Experimental Assay: Tm pH:11.18 ; Experimental Assay: dCp pH:11.49 ; Experimental Assay: dHcal pH:11.49 ; Experimental Assay: Tm pH:11.49 ; Experimental Assay: dCp pH:9.9 ; Experimental Assay: dHcal pH:9.9 ; Experimental Assay: Tm pH:9.9 ; Experimental Assay: dCp pH:10.01 ; Experimental Assay: dHcal pH:10.01 ; Experimental Assay: Tm pH:10.01 ; Experimental Assay: dCp pH:10.32 ; Experimental Assay: dHcal pH:10.32 ; Experimental Assay: Tm pH:10.32 ; Experimental Assay: dCp pH:10.72 ; Experimental Assay: dHcal pH:10.72 ; Experimental Assay: Tm pH:10.72 ; Experimental Assay: dCp pH:10.83 ; Experimental Assay: dHcal pH:10.83 ; Experimental Assay: Tm pH:10.83 ; Experimental Assay: dCp pH:11.2 ; Experimental Assay: dHcal pH:11.2 ; Experimental Assay: Tm pH:11.2 ; Experimental Assay: Tm pH:9.44 ; Experimental Assay: dCp pH:9.87 ; Experimental Assay: dHcal pH:9.87 ; Experimental Assay: Tm pH:9.87 ; Experimental Assay: dCp pH:10.14 ; Experimental Assay: dHcal pH:10.14 ; Experimental Assay: Tm pH:10.14 ; Experimental Assay: dCp pH:10.34 ; Experimental Assay: dHcal pH:10.34 ; Experimental Assay: Tm pH:10.34 ; Experimental Assay: dCp pH:10.76 ; Experimental Assay: dHcal pH:10.76 ; Experimental Assay: Tm pH:10.76 ; Experimental Assay: dCp pH:11.15 ; Experimental Assay: dHcal pH:11.15 ; Experimental Assay: Tm pH:11.15 ; Experimental Assay: dCp pH:11.55 ; Experimental Assay: dHcal pH:11.55 ; Experimental Assay: Tm pH:11.55 ; Experimental Assay: dCp pH:11.69 ; Experimental Assay: dHcal pH:11.69 ; Experimental Assay: Tm pH:11.69 ; Experimental Assay: dCp pH:11.77 ; Experimental Assay: dHcal pH:11.77 ; Experimental Assay: Tm pH:11.77 ; Experimental Assay: dCp pH:8.0 ; Experimental Assay: dHcal pH:8.0 ; Experimental Assay: Tm pH:8.0 ; Experimental Assay: dCp pH:9.94 ; Experimental Assay: dHcal pH:9.94 ; Experimental Assay: Tm pH:9.94 ; Experimental Assay: dCp pH:10.15 ; Experimental Assay: dHcal pH:10.15 ; Experimental Assay: Tm pH:10.15 ; Experimental Assay: dCp pH:10.36 ; Experimental Assay: dHcal pH:10.36 ; Experimental Assay: Tm pH:10.36 ; Experimental Assay: dCp pH:10.71 ; Experimental Assay: dHcal pH:10.71 ; Experimental Assay: Tm pH:10.71 ; Experimental Assay: dCp pH:11.27 ; Experimental Assay: dHcal pH:11.27 ; Experimental Assay: Tm pH:11.27 ; Experimental Assay: dCp pH:11.6 ; Experimental Assay: dHcal pH:11.6 ; Experimental Assay: Tm pH:11.6 ; Experimental Assay: dCp pH:11.85 ; Experimental Assay: dHcal pH:11.85 ; Experimental Assay: Tm pH:11.85 ; Experimental Assay: dCp pH:11.97 ; Experimental Assay: dHcal pH:11.97 ; Experimental Assay: Tm pH:11.97 ; Experimental Assay: dCp pH:9.99 ; Experimental Assay: dHcal pH:9.99 ; Experimental Assay: Tm pH:9.99 ; Experimental Assay: dCp pH:10.18 ; Experimental Assay: dHcal pH:10.18 ; Experimental Assay: Tm pH:10.18 ; Experimental Assay: dCp pH:10.37 ; Experimental Assay: dHcal pH:10.37 ; Experimental Assay: Tm pH:10.37 ; Experimental Assay: dCp pH:10.59 ; Experimental Assay: dHcal pH:10.59 ; Experimental Assay: Tm pH:10.59 ; Experimental Assay: dCp pH:10.87 ; Experimental Assay: dHcal pH:10.87 ; Experimental Assay: Tm pH:10.87 ; Experimental Assay: dCp pH:11.09 ; Experimental Assay: dHcal pH:11.09 ; Experimental Assay: Tm pH:11.09 ; Experimental Assay: dCp pH:11.1 ; Experimental Assay: dHcal pH:11.1 ; Experimental Assay: Tm pH:11.1 ; Experimental Assay: dCp pH:11.92 ; Experimental Assay: dHcal pH:11.92 ; Experimental Assay: Tm pH:11.92 ; Experimental Assay: dCp pH:11.96 ; Experimental Assay: dHcal pH:11.96 ; Experimental Assay: Tm pH:11.96 ; Experimental Assay: Tm pH:9.52 ; Experimental Assay: dCp pH:9.63 ; Experimental Assay: dHcal pH:9.63 ; Experimental Assay: Tm pH:9.63 ; Experimental Assay: dCp pH:9.98 ; Experimental Assay: dHcal pH:9.98 ; Experimental Assay: Tm pH:9.98 ; Experimental Assay: dCp pH:10.38 ; Experimental Assay: dHcal pH:10.38 ; Experimental Assay: Tm pH:10.38 ; Experimental Assay: dCp pH:10.65 ; Experimental Assay: dHcal pH:10.65 ; Experimental Assay: Tm pH:10.65 ; Experimental Assay: dCp pH:10.97 ; Experimental Assay: dHcal pH:10.97 ; Experimental Assay: Tm pH:10.97 ; Experimental Assay: dCp pH:11.19 ; Experimental Assay: dHcal pH:11.19 ; Experimental Assay: Tm pH:11.19 ; Experimental Assay: dCp pH:11.5 ; Experimental Assay: dHcal pH:11.5 ; Experimental Assay: Tm pH:11.5 ; Experimental Assay: dCp pH:9.13 ; Experimental Assay: dHcal pH:9.13 ; Experimental Assay: Tm pH:9.13
Libraries Mutations for sequence GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG ; Mutations for sequence MGLSDGEWQLVLNVWGKVEGDLAGHGQEVLIKLFKNHPETLEKFDKFKHLKSEDEMKGSEDLKKHGNTVLTALGGILKKKGQHAAEIQPLAQSHATKHKIPIKYLEFISEAIIQVLQSKHPGDFGADAQGAMSKALELFRNDIAAKYKELGFQG ; Mutations for sequence MGLSDGEWQLVLNAWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGNILKKKGNHEAELKPLAQSHATKHKISVQFLEFISEAIIQVIQSKHPGDFGGDAQAAMGKALELFRNDMAAKYKELGFQG ; Mutations for sequence MHDAELVLKCWGGVEADFEGTGGEVLTRLFKQHPETQKLFPKFVGIASNELAGNAAVKAHGATVLKKLGELLKARGDHAAILKPLATTHANTHKIALNNFRLITEVLVKVMAEKAGLDAGGQSALRRVMDVVIGDIDTYYKEIGFAG

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
3VM9 2012-09-12 1.05 Dimeric horse myoglobin
4TWV 2016-05-04 1.06 Horse heart myoglobin mutant (K45E/K63E/K96E) with Zn-deuteroporphyrin IX
4TWU 2016-05-04 1.08 Horse heart myoglobin mutant (D44K/D60K/E85K) with Zn-deuteroporphyrin IX
4NS2 2014-12-24 1.18 Crystal structure of Horse heart ferric myoglobin; D44K/D60K/E85K mutant
2V1I 2007-06-12 1.2 Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 6.8
2FRF 2006-05-30 1.2 Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak
2V1F 2007-06-12 1.2 Crystal structure of radiation-induced myoglobin compound II - intermediate H at pH 8.7
5AZR 2016-01-20 1.2 Crystal structure of aqua-cobalt(III) tetradehydrocorrin in the heme pocket of horse heart myoglobin
3RJ6 2012-05-09 1.23 Crystal Structure of Horse heart ferric myoglobin; K45E/K63E/K96E mutant
2V1K 2007-06-12 1.25 Crystal structure of ferrous deoxymyoglobin at pH 6.8
2V1H 2007-06-12 1.3 Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 5.2
3WFT 2014-12-03 1.3 Crystal structure of horse heart myoglobin reconstituted with cobalt(II) tetradehydrocorrin
2FRJ 2006-05-30 1.3 Nitrosyl Horse Heart Myoglobin, Nitrite/Dithionite Method
2V1E 2007-06-12 1.3 Crystal structure of radiation-induced myoglobin compound II - intermediate H at pH 6.8
2FRK 2006-05-30 1.3 Nitrosyl Horse Heart Myoglobin, Nitric Oxide Gas Method
2VLX 2009-02-10 1.3 Crystal structure of peroxymyoglobin generated by cryoradiolytic reduction of myoglobin compound III
1GJN 2002-03-01 1.35 Hydrogen Peroxide Derived Myoglobin Compound II at pH 5.2
2V1G 2007-06-12 1.35 Crystal structure of radiation-induced myoglobin compound II - intermediate H at pH 5.2
3WFU 2014-12-03 1.35 Crystal structure of horse heart myoglobin reconstituted with cobalt(I) tetradehydrocorrin
2V1J 2007-06-12 1.4 Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 8.7
5AZQ 2016-01-20 1.4 Crystal structure of cyano-cobalt(III) tetradehydrocorrin in the heme pocket of horse heart myoglobin
1DWT 2000-03-03 1.4 Photorelaxed horse heart MYOGLOBIN CO complex
5ZZE 2019-02-20 1.42 Crystal structure of horse myoglobin crystallized by ammonium sulfate
1DWS 2000-03-03 1.45 PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)
1DWR 2000-03-03 1.45 MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO
2VLZ 2008-01-29 1.5 Crystal structure of peroxymyoglobin generated by cryoradiolytic reduction of myoglobin compound III
5YL3 2017-12-27 1.5 Crystal structure of horse heart myoglobin reconstituted with manganese porphycene in resting state at pH 8.5
4DC7 2013-01-23 1.5 Crystal Structure of Myoglobin Exposed to Excessive SONICC Imaging Laser Dose.
4DC8 2013-01-23 1.5 Crystal Structure of Myoglobin Unexposed to Excessive SONICC Imaging Laser Dose.
3LR9 2010-07-07 1.55 X-ray photogenerated ferrous horse heart myoglobin, nitrite adduct
5YCJ 2018-09-19 1.58 Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly) imidazole-ligand
2O5S 2007-10-16 1.6 Cobalt horse heart myoglobin, nitrite modified
2VLY 2008-01-29 1.6 Crystal structure of myoglobin compound III (radiation-induced)
2FRI 2006-05-30 1.6 Horse Heart Myoglobin, Nitrite Adduct, Co-crystallized
2O5O 2007-10-16 1.6 Manganese horse heart myoglobin, nitrite modified
5D5R 2015-09-16 1.6 Horse-heart myoglobin - deoxy state
3LR7 2010-07-07 1.6 Ferric horse heart myoglobin, nitrite adduct
2O5T 2007-10-16 1.6 Cobalt horse heart myoglobin, oxidized
1NZ3 2003-04-08 1.6 K45E-K63E Variant of Horse Heart Myoglobin
2VM0 2008-01-29 1.6 Crystal structure of radiation-induced myoglobin compound II generated after annealing of peroxymyoglobin
2O58 2007-10-16 1.65 Horse heart met manganese myoglobin
2O5M 2007-10-16 1.65 Manganese horse heart myoglobin, azide modified
3V2Z 2012-11-21 1.65 Nitrite Bound Chlorin Substituted Myoglobin- Method 2
3V2V 2012-11-21 1.65 Nitrite Bound Chlorin Substituted Myoglobin- Method 1
3RGK 2011-04-27 1.65 Crystal Structure of Human Myoglobin Mutant K45R
3VAU 2012-04-11 1.7 Myoglobin nitrite structure: nitriheme modified
1RSE 1996-12-23 1.7 MYOGLOBIN (HORSE HEART) MUTANT WITH SER 92 REPLACED BY ASP (S92D)
1HRM 1995-01-26 1.7 THE PROXIMAL LIGAND VARIANT HIS93TYR OF HORSE HEART MYOGLOBIN
1XCH 1997-09-17 1.7 MYOGLOBIN (HORSE HEART) MUTANT WITH LEU 104 REPLACED BY ASN (L104N)
2O5L 2007-10-16 1.7 Manganese horse heart myoglobin, methanol modified
1NZ5 2003-04-08 1.7 The Horse heart myoglobin variant K45E/K63E complexed with Manganese
1WLA 1998-01-14 1.7 MYOGLOBIN (HORSE HEART) RECOMBINANT WILD-TYPE
1MWC 1998-08-19 1.7 WILD TYPE MYOGLOBIN WITH CO
1NPG 2003-11-11 1.7 MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITROSOETHANE
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)
5CN9 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0.4 ps time delay
1NZ4 2003-04-08 1.8 The horse heart myoglobin variant K45E/K63E complexed with Cadmium
5CNE 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 10 ps time delay
5CNC 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0.6 ps time delay
5CNB 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0.5 ps time delay
5CNG 2015-09-16 1.8 ultrafast dynamics in myoglobin: 150 ps time delay
5CNF 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 50 ps time delay
1MWD 1998-08-19 1.8 WILD TYPE DEOXY MYOGLOBIN
1BJE 1998-01-28 1.8 H64T VARIANT OF MYOGLOBIN (HORSE HEART) RECOMBINANT WILD-TYPE COMPLEXED WITH AZIDE
3BA2 2008-11-11 1.8 Cyanide bound Chlorin substituted Myoglobin
5CND 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 3 ps time delay
5CN7 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0.2 ps time delay
1M6M 1998-08-19 1.8 V68N MET MYOGLOBIN
5CMV 2015-09-16 1.8 Ultrafast dynamics in myoglobin: dark-state, CO-ligated structure
5CN8 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0.3 ps time delay
5CN5 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0 ps time delay
5CN6 2015-09-16 1.8 Ultrafast dynamics in myoglobin: 0.1 ps time delay
5CN4 2015-09-16 1.8 Ultrafast dynamics in myoglobin: -0.1 ps time delay
5Z7E 2019-01-30 1.8 Horse Heart Myoglobin Mutant - H93M
2O5Q 2007-10-16 1.9 Manganese horse heart myoglobin, nitric oxide modified
1M6C 1998-08-19 1.9 V68N MYOGLOBIN WITH CO
5Z7F 2019-01-30 1.9 Horse Heart Myoglobin Mutant -V68A/I107Y-Sulfide Derivative
2NSR 2007-11-06 1.9 Nitromethane Modified Horse Heart Myoglobin
1NZ2 2003-04-08 1.9 K45E Variant of Horse Heart Myoglobin
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)
1HSY 1995-02-27 1.9 ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS
3HEN 2009-12-29 1.9 Ferric Horse Heart Myoglobin; H64V/V67R Mutant
1YMB 1994-01-31 1.9 HIGH RESOLUTION STUDY OF THE THREE-DIMENSIONAL STRUCTURE OF HORSE HEART METMYOGLOBIN
1NPF 2003-11-11 1.9 MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE
3RJN 2012-05-09 1.9 Horse heart myoglobin: D44K/D60K mutant with zinc (II) -deuteroporphyrin dimethyl ester
1MYJ 1994-01-31 1.9 DISTAL POLARITY IN LIGAND BINDING TO MYOGLOBIN: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A THREONINE68(E11) MUTANT
1MNO 1998-08-19 1.95 V68N MYOGLOBIN OXY FORM
3HEP 2009-12-29 1.95 Ferric Horse Heart Myoglobin; H64V Mutant, Nitrite Modified
5YCI 2018-09-19 1.97 Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly)
1MDN 1998-09-30 1.98 WILD TYPE MYOGLOBIN WITH CO
3HC9 2009-12-29 2.0 Ferric Horse Heart Myoglobin; H64V mutant
3WYO 2014-11-19 2.0 Heterodimeric myoglobin formed by domain swapping
1YMA 1994-01-31 2.0 STRUCTURAL CHARACTERIZATION OF HEME LIGATION IN THE HIS64-->TYR VARIANT OF MYOGLOBIN
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)
2O5B 2007-10-16 2.0 Manganese horse heart myoglobin, reduced
2NSS 2007-11-06 2.0 Nitrobenzene Modified Horse Heart Myoglobin
3HEO 2009-12-29 2.0 Ferric Horse Heart Myoglobin; H64V/V67R mutant, Nitrite Modified
1AZI 1998-02-25 2.0 MYOGLOBIN (HORSE HEART) RECOMBINANT WILD-TYPE COMPLEXED WITH AZIDE
1YMC 1994-01-31 2.0 THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C
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
2IN4 2006-10-31 2.15 Crystal Structure of Myoglobin with Charge Neutralized Heme, ZnDMb-dme
3WI8 2014-03-26 2.2 Crystal structure of horse heart myoglobin reconstituted with manganese porphycene
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
5YCG 2018-09-19 2.4 Ancestral myoglobin aMbWp of Pakicetus relative
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
90.3 Myoglobin P02170 MYG_RABIT
90.3 Myoglobin C0HKB7 MYG_SCIVU
90.3 Myoglobin P02157 MYG_MELME
90.3 Myoglobin P02156 MYG_ERIEU
90.3 Myoglobin P02164 MYG_ORYAF
90.9 Myoglobin P20856 MYG_CTEGU
92.2 Myoglobin P02163 MYG_ROUAE
91.6 Myoglobin P04250 MYG_LAGMA
91.6 Myoglobin C0HJQ9 MYG_HYSCR
92.2 Myoglobin Q6PL31 MYG_OCHCU
92.9 Myoglobin P02165 MYG_TUPGL
92.9 Myoglobin P02189 MYG_PIG
92.9 Myoglobin P04249 MYG_PROGU
93.5 Myoglobin P02171 MYG_OCHPR
94.2 Myoglobin P11343 MYG_LUTLU
100.0 Myoglobin P04248 MYG_SPAEH
90.3 Myoglobin P02150 MYG_MACFA
90.3 Myoglobin P02144 MYG_HUMAN
90.9 Myoglobin P68085 MYG_SEMEN
90.9 Myoglobin P68084 MYG_PAPAN
90.9 Myoglobin P68086 MYG_ERYPA
100.0 Myoglobin P02193 MYG_DIDVI
100.0 Myoglobin P02204 MYG_CYPCA
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 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