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| _ \ ___ | |_ (_) _ __ ___ __| | (_) __ _
| |_) | / _ \ | __| | | | '_ \ / _ \ / _| | | | / _ |
| _ < | __/ | |_ | | | |_) | | __/ | (_| | | | | (_| |
|_| \_\ \___| \__| |_| | .__/ \___| \__,_| |_| \__,_|
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RiAFP
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
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RiAFP ist eine Gruppe von Anti-Frost-Proteinen (AFP) aus dem BockkΓ€fer Rhagium inquisitor. RiAFP(H4) besitzen eine der regelmΓ€Γigsten Proteinstrukturen aller bisher untersuchten Proteine.cite-ref-1[1]
Contents
β’ Eigenschaften
β’ Weblinks
β’ Einzelnachweise
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
Eigenschaften
Die sechs bisher beschriebenen RiAFP besitzen eine Masse von etwa 12,5 bis 12,8 Kilodalton, einen isoelektrischen Punkt oberhalb von acht und mehrere Wiederholungen der AminosΓ€uresequenz TxTxTxT in unregelmΓ€Γigen AbstΓ€nden.cite-ref-2[2]cite-ref-3[3] RiAFP besitzen weiterhin keine Homologien zu bekannten Proteinen.cite-ref-4[4]
Die Anti-Frost-Proteine aus KΓ€fern gehΓΆren zu denen mit der stΓ€rksten WΓ€rmehysteresewirkung, bei Tenebrio molitor ist sie etwa hundertfach stΓ€rker als bei den Anti-Frost-Proteinen aus polaren Fischen und fΓΌhrt in einer Konzentration von 1 mg / ml zu einer Gefrierpunktserniedrigung von 5,5 Β°C.cite-ref-pmid-9285581-5-0[5]
Weblinks
Einzelnachweise
cite-note-11. β A. Hakim, J. B. Nguyen, K. Basu, D. F. Zhu, D. Thakral, P. L. Davies, F. J. Isaacs, Y. Modis, W. Meng: Crystal structure of an insect antifreeze protein and its implications for ice binding. In: The Journal of biological chemistry. Band 288, Nummer 17, April 2013, ISSN 1083-351X, S. 12295β12304, doi:10.1074/jbc.M113.450973, PMID 23486477, PMC 3636913 (freier Volltext).
cite-note-22. β E. Kristiansen, H. RamlΓΈv, L. Hagen, S. A. Pedersen, R. A. Andersen, K. E. Zachariassen: Isolation and characterization of hemolymph antifreeze proteins from larvae of the longhorn beetle Rhagium inquisitor (L.). In: Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology. Band 142, Nummer 1, September 2005, ISSN 1096-4959, S. 90β97, doi:10.1016/j.cbpc.2005.06.004, PMID 15993638.
cite-note-33. β E. Kristiansen, H. RamlΓΈv, P. HΓΈjrup, S. A. Pedersen, L. Hagen, K. E. Zachariassen: Structural characteristics of a novel antifreeze protein from the longhorn beetle Rhagium inquisitor. In: Insect biochemistry and molecular biology. Band 41, Nummer 2, Februar 2011, ISSN 1879-0240, S. 109β117, doi:10.1016/j.ibmb.2010.11.002, PMID 21078390.
cite-note-44. β A. Hakim, D. Thakral, D. F. Zhu, J. B. Nguyen: Expression, purification, crystallization and preliminary crystallographic studies of Rhagium inquisitor antifreeze protein. In: Acta crystallographica. Section F, Structural biology and crystallization communications. Band 68, Pt 5Mai 2012, ISSN 1744-3091, S. 547β550, doi:10.1107/S1744309112010421, PMID 22691785, PMC 3374510 (freier Volltext).