Bioinformatica proteinelor: Mioglobina

Ungurean Livia-Mihaela
Biologia dezvoltrii

Mioglobina
Face parte din familia proteinelor globulare Organism: Homo sapiens, Lungimea secvenei: 154 aminoacizi Funcii: servete ca o surs suplimentar de oxigen i facilteaz trecerea oxigenului prin muchi. Funcii moleculare: protein muscular Procese biologice: transportul oxigenului
Format FASTA mioglobin >sp|P02144|MYG_HUMAN Myoglobin OS=Homo sapiens GN=MB PE=1 SV=2 MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLK KHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKH PGDFGADAQGAMNKALELFRKDMASNYKELGFQG

Alinierea multipl asecvenelor mioglobinei umane i de la celelalte specii alese. Poziiile n care se gsesc aminoacizii conservi 100% este marcat cu semnul *, cele n care se regsesc aminoacizii diferii, dar cu proprieti fizico-chimice similare sunt marcate cu :i respectiv .. Inseriile sunt marcate cu -.

Scorurile de aliniere pentru perechi ale secvenelor mioglobinei umane i a celorlate specii alese. (Blast)
TEMPLATE pdb1ch4A-0 E 1.000000e-63 FIRST 1 LAST 148 ID 25.000000 ALIGNEMENT see alignment COMMENT OXYGEN TRANSPORT 11JUN-98 1CH4 CROSS_PDB OXYGEN TRANSPORT 11JUN-98 1CH4 CROSS_PDB OXYGEN TRANSPORT 11JUN-98 1CH4 CROSS_PDB OXYGEN TRANSPORT 11JUN-98 1CH4 CROSS_PDB OXYGEN TRANSPORT 08DEC-97 1A0U CROSS_PDB NPSA link NPSA

pdb1ch4B-0

1.000000e-63

148

25.000000

see alignment

NPSA

pdb1ch4C-0

1.000000e-63

148

25.000000

see alignment

NPSA

pdb1ch4D-0

1.000000e-63

148

25.000000

see alignment

NPSA

pdb1a0uB-0 1.000000e-62 1 148 25.000000 see alignment

NPSA

Cu ajutorul lui ProtParam s-a generat: Masa molecular: 17183.8Da (dalton) Punct izoelectric: 7.14 Sarcina net: 0 Indexul de instabilitate (II) este 21.81. Acesta clasific proteina ca i stabil. Index alifatic: 84.29 Media hidrocapacitii(GRAVY): -0.476 ProtScale permite reprezentarea profilului produs de scala unui aminoacid asupra proteinei selectate.

Hidrofil (negativ): Arg, Asp, Gln, Gly, Glu, His, Lys, Pro, Thr, Ser, Trp Hidrofob (pozitiv): Ala, Cys, Ile, Leu, Met, Phe, Protein fr tendin de hidrofilie sau hidrofobicitate.Exist cteva poriuni puternic hidrofile sau hidrofobe. Graficul este imaginea n oglind a celuilalt grafic.

La 0,43 (mijlocul graficului) apare cea mai mare flexibilitate care corespunde cu regiunile hidrofile din graficul anterior.
Profilul flexibilitii medii a mioglobinei umane

Regiuni alfa-helix (peste 1): 1-20, 20-70, 80-100, 110-120, 120-140.

Regiunile alfa de deasupra de linia de mijloc sunt imaginea n oglind a imaginii de la grafiucl beta. Regiuni alfa : 40-60, 80-100, 120-140 Regiuni beta: 0,7-20 , 20-40, 100-120 , 120-140

Structura secundar

Jpred: H inseamna elice iar liniua nseamn regiune dezordonat PSIPRED: Regiuni elice: D5-V18, I22- G36, P38-F44, E60-H78, H83-A96, Y105-S119, G126-K19 Acest rezultat este conform i cu prezicerea efectuat cu ajutorul programului anterior.

GlobPlot: prezice regiuni dezordonate

Regiuni dezordonate: 1-5, 19-34, 153-161, 183-187

Analiza regiunilor dezordonate ale mioglobinei umane, cu ajutorul programului RONN

Regiuni dezordonate: 48-67, 75-99

Imaginea a fost generat cu ajutorul programului CHIMERA.

ID

Area
1 540.2 7 1 103.6 6 1 86.6 5 1 85.8 4 1 86.7 3 1 51.1 2 1 55.2 1 1 82.3 0 9 50.8 8 44.3 7 42.6 6 30.4 5 24.1 4 40.9 3 20.7 2 15 1 28.1

Vol
72 9.9 11 2.7 98 65. 4 78. 9 33. 3 60. 8 60. 1 29. 4 41. 6 24. 6 21. 6 17 21. 5 15 10 13. 4

CASTp identific i caracterizeaz caviti situate pe suprafaa proteinelor.

Vizualizarea

cavitilor

mioglobinei

cu

ajutorul

programului

Fpocket.

String:

Determinarea dimensiunii fractale a suprafeei mioglobinei umane

2+0,311

2.311 DIMENNSIUNEA FRACTALA

Programul GETAREA calculeaz aria accesibl solventului pentru protein ca ntreg, pentru fiecare aminoacid n parte, pe categorii de atomi, respectiv pentru fiecare atom.

Referine bibliografice
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