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Titolo:
Recognition between flexible protein molecules: induced and assisted folding
Autore:
Demchenko, AP;
Indirizzi:
TUBITAK, Marmara Res Ctr, TR-41470 Gebze Kocaeli, Turkey TUBITAK Gebze Kocaeli Turkey TR-41470 tr, TR-41470 Gebze Kocaeli, Turkey Ukrainian Acad Sci, Palladin Inst Biochem, UA-252030 Kiev, Ukraine Ukrainian Acad Sci Kiev Ukraine UA-252030 ochem, UA-252030 Kiev, Ukraine
Titolo Testata:
JOURNAL OF MOLECULAR RECOGNITION
fascicolo: 1, volume: 14, anno: 2001,
pagine: 42 - 61
SICI:
0952-3499(200101/02)14:1<42:RBFPMI>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT-SHOCK-PROTEIN; INDUCED CONFORMATIONAL-CHANGES; 2 OVERLAPPING FRAGMENTS; CHAPERONE-LIKE ACTIVITY; HIGH-AFFINITY BINDING; RESOLUTION SOLUTION STRUCTURE; PAIRED HELICAL FILAMENTS; NMR SOLUTION STRUCTURE; X-RAY-DIFFRACTION; ALPHA-CRYSTALLIN;
Keywords:
molecular recognition; flexible molecules; protein-ligand interaction; protein folding; molecular chaperones; folding diseases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
245
Recensione:
Indirizzi per estratti:
Indirizzo: Demchenko, AP TUBITAK, Marmara Res Ctr, TR-41470 Gebze Kocaeli, Turkey TUBITAK Gebze Kocaeli Turkey TR-41470 ebze Kocaeli, Turkey
Citazione:
A.P. Demchenko, "Recognition between flexible protein molecules: induced and assisted folding", J MOL RECOG, 14(1), 2001, pp. 42-61

Abstract

This review focuses on a very important but little understood type of molecular recognition - the recognition between highly flexible molecular structures. The formation of a specific complex in this case is a dynamic process that can occur through sequential steps of mutual conformational adaptation. This allows modulation of specificity and affinity of interaction in extremely broad ranges. The interacting partners can interact together to form a complex with entirely new properties and produce conformational signal transduction at substantial distance. We show that this type of recognitionis frequent in formation of different protein-protein and protein-nucleic acid complexes. It is also characteristic for self-assembly of protein molecules from their unfolded fragments as well as for interaction of molecularchaperones with their substrates and it can be the origin of 'protein misfolding' diseases. Thermodynamic and kinetic features of this type of dynamic recognition and the principles underlying their modeling and analysis arediscussed. Copyright (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 07:29:22