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Folding and amyloid-fibril formation for a series of human stefins' chimeras: any correlation?Kenig, Manca ...To study the influence of whole secondary structure elements to the process offolding and amyloid-fibril formation, chimeras of stefins have been prepared. GdnHCl denaturation curves and folding ... rates (chevron plots) have been analyzed based on a two-state mechanism. The order of stability isČ stefin A > aAbbbb > bAbbbb > stefin B = aBaaaa > bBaaaa, where the make up of chimeric proteins is designated by small letters representing the source of individual strands (a for stefin A, b for stefin B) and a capital letter representing the source of the helix (A for stefin A and B for stefin B). Onlythe fast folding reactions were included in the analysis and it has been found that stefin B folds the fastest (657 s-1). Similarly, fast folders are the chimeric proteins aBaaaa and bBaaaa, both of which contain the -helix of stefin B. Unfolding rates correlate very well with protein stability, with theslowest rate for the most stable protein, stefin A. Amyloid-fibril growth was measured for each protein by monitoring thioflavin T fluorescence and was visualized using electron microscopy. The propensity to form amyloid-fibrils is in the orderČ stefin B > bAbbbb > aAbbbb > bBaaaa > aBaaaa > stefin A. Thisorder does not correlate with stability, or with the folding or unfolding rates. Instead, the propensity to fibrillize is related to selected parts of structure, such as the -sheet of stefin B, and can be predicted reasonably well by calculating the -strand propensity of the denatured states.Vir: Proteins. - ISSN 0887-3585 (Vol. 62, no. 4, 2006, str. 918-927 = Proteins (Online). - ISSN 1097-0134. - str. 918-927)Vrsta gradiva - članek, sestavni delLeto - 2006Jezik - angleškiCOBISS.SI-ID - 3428890
Avtor
Kenig, Manca |
Kokalj-Jenko, Saša, biokemija, 1976- |
Tušek-Žnidarič, Magda |
Pompe Novak, Maruša |
Gunčar, Gregor |
Turk, Dušan, 1959- |
Waltho, Jonathan P. |
Staniforth, Rosemary A. |
Avbelj, Franc, kemik |
Žerovnik, Eva
Teme
amyloid-fibril |
conformational disease |
cystatin |
stefin B |
ionic interactions |
protein aggregation |
protein folding
Vnos na polico
Trajna povezava
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Baze podatkov, v katerih je revija indeksirana
Ime baze podatkov | Področje | Leto |
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Povezave do osebnih bibliografij avtorjev | Povezave do podatkov o raziskovalcih v sistemu SICRIS |
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Kenig, Manca | 19332 |
Kokalj-Jenko, Saša, biokemija, 1976- | 20212 |
Tušek-Žnidarič, Magda | 09864 |
Pompe Novak, Maruša | 18467 |
Gunčar, Gregor | 15639 |
Turk, Dušan, 1959- | 04988 |
Waltho, Jonathan P. | |
Staniforth, Rosemary A. | |
Avbelj, Franc, kemik | 09899 |
Žerovnik, Eva | 03368 |
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