The Myoglobin Protein

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Sequence Alignment of the Myoglobin Protein (with Clustalw) a

Species Sequence Alignment 

Mouse        MGLSDGEWQLVLNVWGKVEADLAGHGQEVLIGLFKTHPETLDKFDKFKNLKSEEDMKGSE 60
Rat          MGLSDGEWQMVLNIWGKVEGDLAGHGQEVLISLFKAHPETLEKFDKFKNLKSEEEMKSSE 60
Human        MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASE 60
Pig          MGLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASE 60
Cow          MGLSDGEWQLVLNAWGKVEADVAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASE 60
Zebrafish    --MAD--HDLVLKCWGAVEADYAANGGEVLNRLFKEYPDTLKLFPKFSGIS-QGDLAGSP 55
               ::*   ::**: ** **.* ..:* ***  **. :*:**. * **. :. : :: .* 

Mouse        DLKKHGCTVLTALGTILKKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEIIIEVLKKRH 120
Rat          DLKKHGCTVLTALGTILKKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEVIIQVLKKRY 120
Human        DLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKH 120
Pig          DLKKHGNTVLTALGGILKKKGHHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKH 120
Cow          DLKKHGNTVLTALGGILKKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHAKH 120
Zebrafish    AVAAHGATVLKKLGELLKAKGDHAALLKPLANTHANIHKVALNNFRLITEVLVKVMAEKA 115
              :  ** ***. ** :** **.* * :  **::**. **:.:: :.:*:: ::.*:  : 

Mouse        SGDFGADAQGAMSKALELFRNDIAAKYKELGFQG 154
Rat          SGDFGADAQGAMSKALELFRNDIAAKYKELGFQG 154
Human        PGDFGADAQGAMNKALELFRKDMASNYKELGFQG 154
Pig          PGDFGADAQGAMSKALELFRNDMAAKYKELGFQG 154
Cow          PSDFGADAQAAMSKALELFRNDMAAQYKVLGFHG 154
Zebrafish    G--LDAAGQGALRRVMDAVIGDIDGYYKEIGFAG 147
                :.* .*.*: :.:: .  *: . ** :** *

Accession Numbers: Human - NP_976312; Mouse - NP_038621; Rat - NP_067599; 
Cow - NP_776306; Pig - NP_999401; Zebrafish - NP_956880 

Predicted General Properties of the Myoglobin Protein  (Homo sapiens) - Primary Sequence Analysis (with ProtParam) b

Number of amino acids: 154 Molecular weight: 17183.8 Theoretical pI: 7.14
Amino acid composition: 
Ala (A) 12 7.8% Arg (R) 2 1.3% Asn (N) 3 1.9% Asp (D) 8 5.2% Cys (C) 1 0.6% Gln (Q) 7 4.5% Glu (E) 14 9.1% Gly (G) 15 9.7% His (H) 9 5.8% Ile (I) 8 5.2% Leu (L) 17 11.0% Lys (K) 20 13.0% Met (M) 4 2.6% Phe (F) 7 4.5% Pro (P) 5 3.2% Ser (S) 7 4.5% Thr (T) 4 2.6% Trp (W) 2 1.3% Tyr (Y) 2 1.3% Val (V) 7 4.5% Asx (B) 0 0.0% Glx (Z) 0 0.0% Xaa (X) 0 0.0%
Total number of negatively charged residues (Asp + Glu): 22 Total number of positively charged residues (Arg + Lys): 22 Atomic composition: Carbon C 774 Hydrogen H 1224 Nitrogen N 210 Oxygen O 222 Sulfur S 5 Formula: C774H1224N210O222S5 Total number of atoms: 2435 Extinction coefficients: Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water. Ext. coefficient 13980 Abs 0.1% (=1 g/l) 0.814, assuming ALL Cys residues appear as half cystines Ext. coefficient 13980 Abs 0.1% (=1 g/l) 0.814, assuming NO Cys residues appear as half cystines Estimated half-life: The N-terminal of the sequence considered is M (Met). The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro). >20 hours (yeast, in vivo). >10 hours (Escherichia coli, in vivo). Instability index: The instability index (II) is computed to be 21.81 This classifies the protein as stable. Aliphatic index: 84.29 Grand average of hydropathicity (GRAVY): -0.476

Bioinformatics References

a Higgins D., Thompson J., Gibson T. Thompson J. D., Higgins D. G., Gibson T. J.(1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting,position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.

b Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A.; Protein Identification and Analysis Tools on the ExPASy Server;
(In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press (2005). pp. 571-607  Full text - Copyright Humana Press.

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Recent Articles on the Myoglobin Protein

PubMed: myoglobin
Effects of Hydration State and Resistance Exercise on Markers of Muscle Damage.
Yamamoto LM, Judelson DA, Farrell MJ, Lee EC, Armstrong LE, Casa DJ, Kraemer WJ, Volek JS, Maresh CM
J Strength Cond Res 
Vagal stimulation suppresses ischemia-induced myocardial interstitial myoglobin release.
Kawada T, Yamazaki T, Akiyama T, Kitagawa H, Shuji S, Mizuno M, Li M, Sugimachi M
Life Sci 
Hemoglobin plus myoglobin concentrations and near infrared light pathlength in phantom and pig hearts determined by diffuse reflectance spectroscopy.
Gussakovsky E, Jilkina O, Yang Y, Kupriyanov V
Anal Biochem 
[Early and late biomarkers of late myocardium necrosis in patients with acute coronary syndrome]
Lik Sprava 
Clinical role of urinary low molecular weight proteins: their diagnostic and prognostic implications.
Guder WG, Hofmann W
Scand J Clin Lab Invest Suppl 
Elevated serum creatinine kinase after craniotomy.
Biswas BK, Prasad S, Rich KM
J Neurosurg Anesthesiol 


 

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