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Titolo:
SPECIFIC RECOGNITION OF COILED COILS BY INFRARED-SPECTROSCOPY - ANALYSIS OF THE 3 STRUCTURAL DOMAINS OF TYPE-III INTERMEDIATE FILAMENT PROTEINS
Autore:
HEIMBURG T; SCHUENEMANN J; WEBER K; GEISLER N;
Indirizzi:
MAX PLANCK INST BIOPHYS CHEM,DEPT SPECT D-37018 GOTTINGEN GERMANY MAX PLANCK INST BIOPHYS CHEM,DEPT BIOCHEM D-37018 GOTTINGEN GERMANY
Titolo Testata:
Biochemistry
fascicolo: 5, volume: 35, anno: 1996,
pagine: 1375 - 1382
SICI:
0006-2960(1996)35:5<1375:SROCCB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; NEUROFILAMENT ARCHITECTURE; SECONDARY STRUCTURE; NETWORK FORMATION; TRIPLET PROTEINS; MUSCLE DESMIN; CROSS-LINKING; CYTOCHROME-C; HEAD DOMAIN; ROD DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
T. Heimburg et al., "SPECIFIC RECOGNITION OF COILED COILS BY INFRARED-SPECTROSCOPY - ANALYSIS OF THE 3 STRUCTURAL DOMAINS OF TYPE-III INTERMEDIATE FILAMENT PROTEINS", Biochemistry, 35(5), 1996, pp. 1375-1382

Abstract

The central domain of cytoplasmic intermediate filament (IF) proteinsfrom vertebrates contains some 310 residues and forms a double-stranded coiled coil (rod) with a length of about 46 nm. The flanking terminal domains show a high cell type specific variability both in sequenceand in length. Using Fourier transform infrared (FTIR) spectroscopy we measured secondary structures of isolated domains of type III and IVIF proteins and of the soluble tetramers and the filaments formed by type III IF proteins. The amide I spectrum of the desmin rod is virtually identical to the spectra of other coiled-coil proteins such as tropomyosin and the myosin rod. All these double-stranded coiled coils reveal spectra distinctly different from classical alpha-helical spectra. The spectrum of coiled coils is a triplet of approximately equally strong bands. One band occurs at normal alpha-helix position, while theother two are found at lower wavenumbers. Theoretical aspects of these findings are discussed in the accompanying paper by W. C. Reisdorf and S. Krimm [(1996) Biochemistry 35, 1383-1386]. The amino-terminal head domain of desmin has a multicomponent spectrum with major fractionsof beta-sheet. The carboxy-terminal tail domains of desmin and the neurofilament proteins L and H, the latter in the phosphorylated and in the dephosphorylated forms, have very similar FTIR spectra, indicatingmostly random structure. The spectrum of desmin type III protofilaments is very similar to the sum of the spectra of the three isolated domains. Polymerization into filaments seems to induce a small change in secondary structure.

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Documento generato il 02/04/20 alle ore 19:06:16