Sequence-dependent Stability Of The Beta-helical Fold
نویسندگان
چکیده
منابع مشابه
A Ca2+-dependent bacterial antifreeze protein domain has a novel beta-helical ice-binding fold.
AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large(>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned,expressed and characterized a 322-amino-acid ...
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The Triple β-Spiral is a novel protein structure that plays a role in viral attachment and pathogenesis. At present, there are two Triple β-Spiral structures with solved crystallographic coordinates – one from Adenovirus and the other from Reovirus. There is evidence that the fold also occurs in Bacteriophage SF6. In this thesis, we present a computational analysis of the Triple β-Spiral fold. ...
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متن کاملA Ca2+-dependent bacterial antifreeze protein domain has a novel β-helical ice-binding fold
AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large (>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned, expressed and characterized a 322-amino-aci...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2009
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.12.304