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Titolo:
IMMUNOGLOBULIN-TYPE DOMAINS OF TITIN ARE STABILIZED BY AMINO-TERMINALEXTENSION
Autore:
POLITOU AS; GAUTEL M; JOSEPH C; PASTORE A;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,MEYERHOFSTR 1 D-69117 HEIDELBERG GERMANY EUROPEAN MOLEC BIOL LAB D-69117 HEIDELBERG GERMANY
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 352, anno: 1994,
pagine: 27 - 31
SICI:
0014-5793(1994)352:1<27:IDOTAS>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN; FIBRONECTIN; SEQUENCE; MODULES;
Keywords:
MODULAR PROTEIN; MUSCLE PROTEIN; BOUNDARY; PROTEIN STABILITY; CONNECTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
A.S. Politou et al., "IMMUNOGLOBULIN-TYPE DOMAINS OF TITIN ARE STABILIZED BY AMINO-TERMINALEXTENSION", FEBS letters, 352(1), 1994, pp. 27-31

Abstract

We have recently suggested that similarly folded titin modules located at different sarcomeric regions have distinct molecular properties and stability. Could our selection of module boundaries have potentially influenced our conclusions? To address this question we expressed amino-terminally extended versions of the same modules and determined, with the use of CD and Fluorescence techniques, key thermodynamic parameters characterizing their stability. We present here our results which confirm our previous observations and show that, while amino-terminal extension has a profound effect on the stability of individual modules, it does not affect at all their folding pattern or their relative stabilities. Moreover, our data suggest that the selection of module boundaries can be of critical importance for the structural analysis ofmodular proteins in general, especially when a well-defined intron-exon topography is absent and proteolytic methods are inconclusive.

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Documento generato il 26/11/20 alle ore 20:19:50