Die Natur der Protein-Protein-Wechselwirkung und ihr spektroskopischer Nachweis, dargestellt am Beispiel der Polyglycin-Insulin-Aggregate

Autor:	G. Losse, Heike Noack, Klaus Herzog, Achim Mehlhorn
Rok vydání:	2010
Předmět:	Scope (project management) Chemistry Computational chemistry Stereochemistry Intermolecular force Resolution (electron density) General Chemistry Spectroscopy
Zdroj:	Zeitschrift für Chemie. 30:240-245
ISSN:	0044-2402
DOI:	10.1002/zfch.19900300703
Popis:	Weak intermolecular interactions between proteins may lead to mutual adaption of their secondary structures with the consequence of modified bioactivities. The basic possibilities of protein-protein interactions are summarized in the light of their quantumchemically elucidated nature as well as their spectroscopic indications including modern mathematical tools for artficial resolution enhancement. In this way a clear differentiation between a mixture of proteins and their definite aggregates (complexes) becomes feasible. The example of insulin-polyglycine mixtures and complexes is used to demonstrate scope and limitations of the FT-IR spectroscopy in recognizing and interpreting protein-protein interactions.
Databáze:	OpenAIRE
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