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Titolo:
Designed protein G core variants fold to native-like structures: Sequence selection by ORBIT tolerates variation in backbone specification
Autore:
Ross, SA; Sarisky, CA; Su, A; Mayo, SL;
Indirizzi:
CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 ard Hughes Med Inst, Pasadena, CA 91125 USA CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA CALTECH Pasadena CAUSA 91125 iv Chem & Chem Engn, Pasadena, CA 91125 USA CALTECH, Div Phys Math & Astron, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 Phys Math & Astron, Pasadena, CA 91125 USA CALTECH, Div Biol, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125CALTECH, Div Biol, Pasadena, CA 91125 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 2, volume: 10, anno: 2001,
pagine: 450 - 454
SICI:
0961-8368(200102)10:2<450:DPGCVF>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN-BINDING DOMAIN; DEAD-END ELIMINATION; DISTANCE GEOMETRY; NMR; FLEXIBILITY; STABILITY; PACKING; PROGRAM;
Keywords:
protein design; backbone design; core sidechain packing; dead-end elimination; ORBIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Mayo, SL CALTECH, Howard Hughes Med Inst, Mail Code 147-75, Pasadena, CA 91125 USA CALTECH Mail Code 147-75 Pasadena CA USA 91125 dena, CA 91125 USA
Citazione:
S.A. Ross et al., "Designed protein G core variants fold to native-like structures: Sequence selection by ORBIT tolerates variation in backbone specification", PROTEIN SCI, 10(2), 2001, pp. 450-454

Abstract

The solution structures of two computationally designed core variants of the pi domain of streptococcal protein G (GP1) were solved by H-1 NMR methods to assess the robustness of amino acid sequence selection by the ORBIT protein design package under changes in protein backbone specification. One variant has mutations at three of 10 core positions and corresponds to minimal perturbations of the native GP1 backbone. The other, with mutations at six of 10 positions, was calculated for a backbone in which the separation between G beta1's alpha -helix and beta -sheet was increased by 15% relativeto native G beta1. Exchange broadening of some resonances and the completeabsence of others in spectra of the sixfold mutant bespeak conformational heterogeneity in this protein. The NMR data were sufficiently abundant, however, to generate structures of similar, moderately high quality for both variants. Both proteins adopt backbone structures similar to their target folds. Moreover, the sequence selection algorithm successfully predicted all core chi (1) angles in both variants, five of six chi (2) angles in the threefold mutant and four of seven chi (2) angles in the sixfold mutant. We conclude that ORBIT calculates sequences that fold specifically to a geometryclose to the template, even when the template is moderately perturbed relative to a naturally occurring structure. There are apparently limits to thesize of acceptable perturbations: In this study, the larger perturbation led to undesired dynamic behavior.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 17:52:46