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Spectroscopic analysis of the intera...

Payne, John Carroll.

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Spectroscopic analysis of the interactions between lead and structural zinc-binding domains.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Spectroscopic analysis of the interactions between lead and structural zinc-binding domains./
作者:	Payne, John Carroll.
面頁冊數:	171 p.
附註:	Adviser: Hilary Arnold Godwin.
Contained By:	Dissertation Abstracts International63-04B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3050571
ISBN:	0493651829

Spectroscopic analysis of the interactions between lead and structural zinc-binding domains.
Payne, John Carroll.

Spectroscopic analysis of the interactions between lead and structural zinc-binding domains. - 171 p.

Adviser: Hilary Arnold Godwin.

Thesis (Ph.D.)--Northwestern University, 2002.

To gain a better understanding of the molecular mechanism of lead poisoning, we have investigated the interactions between lead and the metal-binding sites commonly found in zinc proteins. Lead binding to structural zinc-binding sites can be directly observed by monitoring the emergence of intense absorption bands in the near-UV region of the electromagnetic spectrum. These absorption bands are attributable to a combination of S<super>−</super> → Pb(II) ligand-to-metal charge-transfer and lead intraatomic transitions. The emergence of these high-intensity absorption bands provides a sensitive technique to determine the binding affinity of lead(II) to proteins that feature cysteine-rich metal-binding sites.

ISBN: 0493651829Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Spectroscopic analysis of the interactions between lead and structural zinc-binding domains.
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100 1 $a Payne, John Carroll. $3 1259087
245 1 0 $a Spectroscopic analysis of the interactions between lead and structural zinc-binding domains.
300 $a 171 p.
500 $a Adviser: Hilary Arnold Godwin.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1840.
502 $a Thesis (Ph.D.)--Northwestern University, 2002.
520 $a To gain a better understanding of the molecular mechanism of lead poisoning, we have investigated the interactions between lead and the metal-binding sites commonly found in zinc proteins. Lead binding to structural zinc-binding sites can be directly observed by monitoring the emergence of intense absorption bands in the near-UV region of the electromagnetic spectrum. These absorption bands are attributable to a combination of S<super>−</super> → Pb(II) ligand-to-metal charge-transfer and lead intraatomic transitions. The emergence of these high-intensity absorption bands provides a sensitive technique to determine the binding affinity of lead(II) to proteins that feature cysteine-rich metal-binding sites.
520 $a Metal-binding titrations performed on a series of zinc finger consensus peptides (CP-CCHH, CP-CCHC, CP-CCCC) and on a Cys2HisCys zinc-binding domain from the HIV-nucleocapsid protein (HIV-CCHC) indicate that lead possesses a high degree of affinity for zinc-binding sites that are cysteine-rich (K d<super>pb(II)</super> = 10<super>−9</super> to 10<super>−14 </super> M), and lead binds more tightly than zinc does to the Cys4 zinc finger peptide. Furthermore, circular dichroism and NMR studies reveal that the lead-bound forms of each peptide do not adopt the same secondary structure as the zinc-bound peptide. These results suggest that lead may target members of the nuclear hormone receptor superfamily since the DNA-binding domain of each member of this protein family contains two tandem Cys 4 structural zinc-binding sites.
520 $a The thermodynamics of metal binding to the DNA-binding domain of a member of the nuclear hormone receptor superfamily, human estrogen receptor α (hERα DBD), were investigated. Metal binding occurs in a thermodynamically sequential fashion at the Cys4 sites, and lead binds to the protein's Cys4 metal-binding sites with an affinity that is comparable to that of zinc (Kd<super>pb(II)</super> &sim; K d<super>Zn(II)</super> &sim; 10<super>−10</super> M). However, lead does not stabilize the correct fold of the domain, and lead inhibits the DNA-binding activity of the domain. Lead inhibition of members of the nuclear hormone receptor superfamily may explain in part the adverse symptoms observed in individuals suffering from lead poisoning.
590 $a School code: 0163.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Inorganic. $3 517253
690 $a 0487
690 $a 0488
710 2 0 $a Northwestern University. $3 1018161
773 0 $t Dissertation Abstracts International $g 63-04B.
790 $a 0163
790 1 0 $a Godwin, Hilary Arnold, $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3050571