Abstract：
:Spectrin repeats fold into triple helical coiled-coils comprising approximately 106 amino acid residues. Using an AFM-related technique we measured the force required to mechanically unfold these repeats to be 25 to 35 pN. Under tension, individual spectrin repeats unfold independently and in an all-or-none process. The dependence of the unfolding forces on the pulling speed reveals that the corresponding unfolding potential is shallow with an estimated width of 1.5 nm. When the unfolded polypeptide strand is relaxed, several domains refold within less than a second. The unfolding forces of the alpha-helical spectrin domains are five to ten times lower than those found in domains with beta-fold, like immunoglobulin or fibronectin Ill domains, where the tertiary structure is stabilized by hydrogen bonds between adjacent strands. This shows that the forces stabilizing the coiled-coil lead to a mechanically much weaker structure than multiple hydrogen-bonded beta-sheets.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Rief M,Pascual J,Saraste M,Gaub HEdoi
10.1006/jmbi.1998.2466subject
Has Abstractpub_date
1999-02-19 00:00:00pages
553-61issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(98)92466-4journal_volume
286pub_type
杂志文章abstract：:Two-dimensional (15)N-heteronuclear single-quantum coherence (HSQC) NMR studies with a di-domain (lipoyl domain+ linker+ peripheral subunit-binding domain) of the dihydrolipoyl acetyltransferase (E2) component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus allowed a molecular comparison of the ne...
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journal_title：Journal of molecular biology
pub_type： 杂志文章
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pub_type： 杂志文章
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journal_title：Journal of molecular biology
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journal_title：Journal of molecular biology
pub_type： 杂志文章,评审
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journal_title：Journal of molecular biology
pub_type： 杂志文章,评审
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doi：10.1006/jmbi.1997.1021
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doi：10.1006/jmbi.1996.0135
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journal_title：Journal of molecular biology
pub_type： 杂志文章
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journal_title：Journal of molecular biology
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journal_title：Journal of molecular biology
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更新日期：1992-03-05 00:00:00
