کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10804277 | 1057220 | 2011 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Pea lectin unfolding reveals a unique molten globule fragment chain
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کلمات کلیدی
NBSPSLGdnHClN-bromosuccinimideREEs8-anilino-1-naphthalenesulfonatePea lectinTryptophan modification - اصلاح تریپتوفانEquilibrium unfolding - تعادل باز می شودRed edge excitation shift - تغییر لبه سرخ لبهANS - سالPhosphorescence - فسفرانسنسFluorescence - فلورسنسhigh performance liquid chromatography - کروماتوگرافی مایع با کارایی بالاHPLC - کروماتوگرافی مایعی کاراGuanidine hydrochloride - گوانیدین هیدروکلراید
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Pea lectin unfolding reveals a unique molten globule fragment chain Pea lectin unfolding reveals a unique molten globule fragment chain](/preview/png/10804277.png)
چکیده انگلیسی
Pea lectin (PSL) is a dimeric protein in which each subunit comprises two intertwined, post-translationally processed polypeptide chains -a long β-fragment and a short α-fragment. Using guanidine hydrochloride-induced denaturation, we have investigated and characterized the species obtained in the unfolding equilibrium of PSL by steady-state and time-resolved fluorescence, phosphorescence, and selective chemical modification. During unfolding, the fragment chains become separated, and the unfolding pattern reveals a β-fragment as intermediate that has the molten globule characteristics. As examined by 8-anilino-1-naphthalenesulfonate (ANS) binding, the fragment intermediate shows â¼Â 20 fold increase in ANS fluorescence, and a large increase in ANS lifetime (12.8 ns). The tryptophan environment of the molten globule β-fragment has been probed by selective modification with N-bromosuccinimide (NBS), which shows that two tryptophans, possibly Trp 53 and Trp 152 are oxidized while the other Trp 128 remains resistant to oxidation. The different types of tryptophan environment for the intermediate are supported by phosphorescence studies at 77 K, which gives a (0,0) band at 410 nm. These results seem to indicate that the larger fragment chain of PSL can independently behave as a monomeric or single domain protein that undergoes unfolding through intermediate state(s), and may provide important insight into the folding problem of oligomeric proteins in general and lectins in particular.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 93, Issue 3, March 2011, Pages 409-417
Journal: Biochimie - Volume 93, Issue 3, March 2011, Pages 409-417
نویسندگان
Debasish Sen, Dipak K. Mandal,