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Structural studies on the C-terminal...

Luo, Bing-Hao.

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Structural studies on the C-terminal region of beta-spectrin.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Structural studies on the C-terminal region of beta-spectrin./
作者:	Luo, Bing-Hao.
面頁冊數:	125 p.
附註:	Director: Leslie W.-M.Fung.
Contained By:	Dissertation Abstracts International63-01B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3039291
ISBN:	0493527931

Structural studies on the C-terminal region of beta-spectrin.
Luo, Bing-Hao.

Structural studies on the C-terminal region of beta-spectrin. - 125 p.

Director: Leslie W.-M.Fung.

Thesis (Ph.D.)--Loyola University of Chicago, 2002.

Many hereditary hemolytic anemias are due to spectrin abnormalities at the C-terminal region of β-spectrin (the βC region) that destabilize human erythrocyte spectrin tetramer formation.

ISBN: 0493527931Subjects--Topical Terms:

1019105
Biophysics, General.

Structural studies on the C-terminal region of beta-spectrin.
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100 1 $a Luo, Bing-Hao. $3 1259013
245 1 0 $a Structural studies on the C-terminal region of beta-spectrin.
300 $a 125 p.
500 $a Director: Leslie W.-M.Fung.
500 $a Source: Dissertation Abstracts International, Volume: 63-01, Section: B, page: 0244.
502 $a Thesis (Ph.D.)--Loyola University of Chicago, 2002.
520 $a Many hereditary hemolytic anemias are due to spectrin abnormalities at the C-terminal region of β-spectrin (the βC region) that destabilize human erythrocyte spectrin tetramer formation.
520 $a In the first part of the project, I have prepared four recombinant β-peptides of human erythrocyte spectrin of different lengths, all starting at position 1898 of the C-terminal region, but terminating at position 2070, 2071, 2072 or 2073. Results showed that the β-peptides ending prior to residue 2072 (Thr) would not associate with α-peptide, and that no helical bundling of the partial domains was observed. Thus, we suggest that the C-terminal segment of β-spectrin, starting from residue 2073 (Thr), is not critical to spectrin tetramer formation. However, the C-terminal region ending with residue 2072 is important for its association with α-spectrin to form tetramers.
520 $a In the second part of the project, I prepared ten single-cysteine Spα1–368 peptides with cysteine scanning positions 21–30, and twenty-seven single-cysteine Spβ1898–2083 peptides with cysteines scanning positions 2009–2018 and 2060–2076. Results showed that residues at positions 24 and 28 of α-spectrin and at positions 2011, 2014 and 2018 as well as at positions 2061, 2065, 2068, 2069 and 2071 of β-spectrin are important for spectrin tetramerization. The residues 21–30 of α-spectrin are in helical conformation (Helix C<super>′</super>). Disulfide bond formation and cross-linking results are consistent with helical conformations for regions consisting of residues 2009–2018 (Helix A<super>′</super>) and of residues 2060–2073 (Helix B<super>′</super>). We suggest that residues α21, β2011 and β2072 aligned to form a three helical bundle in αN/βC region of spectrin tetramer, and all three residues are in the “a” position of <italic>abcdefg</italic> heptad. Our data also suggest that the conformations of Helix A<super>′</super> and Helix B<super>′</super> in this αβ complex differ from each other.
520 $a In the last part of the project, circular dichroism (CD) and spin labeling electron paramagnetic resonance (EPR) were used to determine the secondary structure of the C-terminal region (residues 2008–2018 and 2060–2076) of β-spectrin in the absence of the α-partner. Combining both EPR and CD data, we suggested that the partial domain of the C-terminal regions of β-spectrin have two unassociated and asymmetric helics. The origin of the asymmetry is not yet clear at present, but we speculate that these helics are curved helics similar to those in coiled coil helices. (Abstract shortened by UMI.)
590 $a School code: 0112.
650 4 $a Biophysics, General. $3 1019105
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791 $a Ph.D.
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