A combinatorial approach to minimal peptide models of a metalloprotein active site.

A combinatorial approach to minimal peptide models of a metalloprotein active site. Research Abstract Details 

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A combinatorial approach to minimal peptide models of a metalloprotein active site. Abstract Text:

Frances Namuswe,David P Goldberg,

Screening of a "one-bead-one-compound" peptide library containing biomimetic His/Cys ligands has led to the discovery of sequences that hydrolyze ester substrates in combination with Zn2+.

A combinatorial approach to minimal peptide models of a metalloprotein active site. Publishing Authors By Initials

F Namuswe,DP Goldberg,

For similar inorganic chemicals: elements: metals, heavy: zinc research abstracts see: inorganic chemicals: elements: metals, heavy: zinc research

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A combinatorial approach to minimal peptide models of a metalloprotein active site. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Chemical communications (Cambridge, England)

VOLUME:

Page Numbers: 2326-8

Journal Abbreviation: Chem. Commun. (Camb.)

ISSN: 1359-7345

DAY: 11

MONTH: 04

YEAR: 2006

A combinatorial approach to minimal peptide models of a metalloprotein active site. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9610838

A combinatorial approach to minimal peptide models of a metalloprotein active site. Keywords Mesh Terms:

KEYWORDS: Zinc

MESH TERMS: chemistry

Chemical & Substance for Abstract: A combinatorial approach to minimal peptide models of a metalloprotein active site. Information

Substance Name: 4-nitrophenyl acetate

Registry Number: 830-03-5

Grant and Affiliation Information for A combinatorial approach to minimal peptide models of a metalloprotein active site.

AFFILIATION: Department of Chemistry, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM62309

ACRONYM: GM

MEDLINETA: Chem Commun (Camb)

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