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Phosphorus containing amino acids: S...

Drabik, Sandra Jean.

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Phosphorus containing amino acids: Synthesis, structural studies, and biomedical applications.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Phosphorus containing amino acids: Synthesis, structural studies, and biomedical applications./
作者:	Drabik, Sandra Jean.
面頁冊數:	239 p.
附註:	Source: Dissertation Abstracts International, Volume: 58-04, Section: B, page: 1883.
Contained By:	Dissertation Abstracts International58-04B.
標題:	Chemistry, Organic. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9730940
ISBN:	0591403382

Phosphorus containing amino acids: Synthesis, structural studies, and biomedical applications.
Drabik, Sandra Jean.

Phosphorus containing amino acids: Synthesis, structural studies, and biomedical applications. - 239 p.

Source: Dissertation Abstracts International, Volume: 58-04, Section: B, page: 1883.

Thesis (Ph.D.)--Washington University, 1997.

A series of phosphine-containing amino acid building blocks were synthesized by a variety of modern synthetic methods. The amino acids were then incorporated into peptides of varying lengths by standard peptide coupling procedures. Two phosphine groups were placed into each peptide chain. The diphosphine peptides were screened as possible biomedical imaging agents by examining their coordination to a variety of transition metals, and characterizing the metal complexes. In order to investigate structure implications of metal binding, a peptide with a high propensity for a reverse turn structure was designed and synthesized. The secondary structure was confirmed by a variety of two dimensional NMR experiments. The effect of metal binding and removal was investigated.

ISBN: 0591403382Subjects--Topical Terms:

516206
Chemistry, Organic.

Phosphorus containing amino acids: Synthesis, structural studies, and biomedical applications.
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520 $a A series of phosphine-containing amino acid building blocks were synthesized by a variety of modern synthetic methods. The amino acids were then incorporated into peptides of varying lengths by standard peptide coupling procedures. Two phosphine groups were placed into each peptide chain. The diphosphine peptides were screened as possible biomedical imaging agents by examining their coordination to a variety of transition metals, and characterizing the metal complexes. In order to investigate structure implications of metal binding, a peptide with a high propensity for a reverse turn structure was designed and synthesized. The secondary structure was confirmed by a variety of two dimensional NMR experiments. The effect of metal binding and removal was investigated.
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