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Titolo:
Synthesis and conformational analysis of the insulin-like 4 gene product
Autore:
Bullesbach, EE; Schwabe, C;
Indirizzi:
Med Univ S Carolina, Dept Biochem & Mol Biol, Charleston, SC 29425 USA MedUniv S Carolina Charleston SC USA 29425 iol, Charleston, SC 29425 USA
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 1, volume: 57, anno: 2001,
pagine: 77 - 83
SICI:
1397-002X(200101)57:1<77:SACAOT>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHASE PEPTIDE-SYNTHESIS; PARTIALLY FOLDED STATE; GROWTH FACTOR-I; HUMAN RELAXIN; RECEPTOR-BINDING; TRIFLUOROETHANOL; SUPERFAMILY; EXPRESSION; MEMBER; 1.5-A;
Keywords:
disulfide synthesis; early placenta insulin-like peptide; EPIL; INSL-4; insulin superfamily; peptide synthesis; relaxin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Bullesbach, EE Med Univ S Carolina, Dept Biochem & Mol Biol, 173 Ashley Ave,POB 250509, Charleston, SC 29425 USA Med Univ S Carolina 173 Ashley Ave,POB 250509 Charleston SC USA 29425
Citazione:
E.E. Bullesbach e C. Schwabe, "Synthesis and conformational analysis of the insulin-like 4 gene product", J PEPT RES, 57(1), 2001, pp. 77-83

Abstract

Insulin-like 4 (INSL-4) is a protein expressed in the early placenta. its primary structure is insulin-like with reference to the distribution of cysteine residues and the single chain proform. Insulin-like 4 was generated by solid-phase peptide synthesis of the two chains followed by the sequential synthesis of the three disulfide bonds. Two disulfide isomers were produced, one with an insulin-like disulfide bonding pattern and the other with areversed chain orientation. The CD spectra of the two disulfide isomers were indistinguishable without any features produced by periodic structures. In addition, the hydrodynamic properties of the two isomers were identical which implied a very open structure of the disulfide-bonded two-chain molecules. It appears that insulin-likeness cannot be defined solely on the basis of the primary structure of cDNA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 10:04:17