کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1985544 1540227 2016 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Transient structures of keratins from hoof and horn influence their self association and supramolecular assemblies
ترجمه فارسی عنوان
ساختارهای گذرا از کراتین ها از گوسفند و شاخ بر ترکیب خود و مجموعه های فوق مولکولی تأثیر می گذارند
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی
Keratins as fibrous proteins, offer structural integrity to various tissues in providing the functional role of protection or load bearing. This work is a prelude to understand the structure − property correlation for a wide variety of keratins. The kinetics of aggregation of bovine hoof keratin (KF) and horn keratin (KR) were monitored by different biophysical methods. pH dependent studies indicated that initially both keratins existed in pre-aggregated form and the efficiency of aggregation decreased with increasing pH. The size of the aggregates was found to be larger in KF compared to KR. UV-vis and particle size analysis clearly revealed that the pre-aggregated forms of KF and KR dissociated to intermediate transient structures with smaller aggregate size, which acted as stronger nucleating agents for further self association of the keratins to form higher order supramolecular assemblies. Conformational analysis indicated that there was no significant conformational change during the aggregation of KF and KR. Morphology of the KF aggregates showed fractal arrangement while KR aggregates formed an ordered structure with no particular arrangement. To the best of our knowledge, this is the first report which shows an interesting and unique observation on changes in the structure during self-association of keratins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 93, Part A, December 2016, Pages 172-178
نویسندگان
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