Tampere University of Technology

TUTCRIS Research Portal

Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms

Research output: Contribution to journalArticleScientificpeer-review

Standard

Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms. / Tossavainen, Helena; Helppolainen, Satu H.; Määttä, Juha A E; Pihlajamaa, Tero; Hytönen, Vesa P.; Kulomaa, Markku S.; Permi, Perttu.

In: BIOMOLECULAR NMR ASSIGNMENTS, Vol. 7, No. 1, 04.2013, p. 35-38.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Tossavainen, H, Helppolainen, SH, Määttä, JAE, Pihlajamaa, T, Hytönen, VP, Kulomaa, MS & Permi, P 2013, 'Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms', BIOMOLECULAR NMR ASSIGNMENTS, vol. 7, no. 1, pp. 35-38. https://doi.org/10.1007/s12104-012-9371-4

APA

Tossavainen, H., Helppolainen, S. H., Määttä, J. A. E., Pihlajamaa, T., Hytönen, V. P., Kulomaa, M. S., & Permi, P. (2013). Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms. BIOMOLECULAR NMR ASSIGNMENTS, 7(1), 35-38. https://doi.org/10.1007/s12104-012-9371-4

Vancouver

Tossavainen H, Helppolainen SH, Määttä JAE, Pihlajamaa T, Hytönen VP, Kulomaa MS et al. Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms. BIOMOLECULAR NMR ASSIGNMENTS. 2013 Apr;7(1):35-38. https://doi.org/10.1007/s12104-012-9371-4

Author

Tossavainen, Helena ; Helppolainen, Satu H. ; Määttä, Juha A E ; Pihlajamaa, Tero ; Hytönen, Vesa P. ; Kulomaa, Markku S. ; Permi, Perttu. / Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms. In: BIOMOLECULAR NMR ASSIGNMENTS. 2013 ; Vol. 7, No. 1. pp. 35-38.

Bibtex - Download

@article{bf18dfee74384e2788a7790a75d95e29,
title = "Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms",
abstract = "Avidin is a homotetrameric ~56 kDa protein found in chicken egg white. Avidin's ability to bind biotin with a very high affinity has widely been exploited in biotechnological applications. Protein engineering has further diversified avidin's feasibility. ChiAVD(I117Y) is a product of rational protein engineering. It is a hyperthermostable synthetic hybrid of avidin and avidin-related protein 4 (AVR4). In this chimeric protein a 23-residue segment in avidin has been replaced with the corresponding sequence found in AVR4, and a point mutation at subunit interface 1-3 (and 2-4) has been introduced. Here we report the backbone and sidechain resonance assignments of the biotin-bound form of ChiAVD(I117Y) as well as the backbone resonance assignments of the free form.",
keywords = "Biotin, Chimeric avidin, Ligand binding, NMR, Thermostability",
author = "Helena Tossavainen and Helppolainen, {Satu H.} and M{\"a}{\"a}tt{\"a}, {Juha A E} and Tero Pihlajamaa and Hyt{\"o}nen, {Vesa P.} and Kulomaa, {Markku S.} and Perttu Permi",
year = "2013",
month = "4",
doi = "10.1007/s12104-012-9371-4",
language = "English",
volume = "7",
pages = "35--38",
journal = "BIOMOLECULAR NMR ASSIGNMENTS",
issn = "1874-2718",
publisher = "Springer Verlag",
number = "1",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms

AU - Tossavainen, Helena

AU - Helppolainen, Satu H.

AU - Määttä, Juha A E

AU - Pihlajamaa, Tero

AU - Hytönen, Vesa P.

AU - Kulomaa, Markku S.

AU - Permi, Perttu

PY - 2013/4

Y1 - 2013/4

N2 - Avidin is a homotetrameric ~56 kDa protein found in chicken egg white. Avidin's ability to bind biotin with a very high affinity has widely been exploited in biotechnological applications. Protein engineering has further diversified avidin's feasibility. ChiAVD(I117Y) is a product of rational protein engineering. It is a hyperthermostable synthetic hybrid of avidin and avidin-related protein 4 (AVR4). In this chimeric protein a 23-residue segment in avidin has been replaced with the corresponding sequence found in AVR4, and a point mutation at subunit interface 1-3 (and 2-4) has been introduced. Here we report the backbone and sidechain resonance assignments of the biotin-bound form of ChiAVD(I117Y) as well as the backbone resonance assignments of the free form.

AB - Avidin is a homotetrameric ~56 kDa protein found in chicken egg white. Avidin's ability to bind biotin with a very high affinity has widely been exploited in biotechnological applications. Protein engineering has further diversified avidin's feasibility. ChiAVD(I117Y) is a product of rational protein engineering. It is a hyperthermostable synthetic hybrid of avidin and avidin-related protein 4 (AVR4). In this chimeric protein a 23-residue segment in avidin has been replaced with the corresponding sequence found in AVR4, and a point mutation at subunit interface 1-3 (and 2-4) has been introduced. Here we report the backbone and sidechain resonance assignments of the biotin-bound form of ChiAVD(I117Y) as well as the backbone resonance assignments of the free form.

KW - Biotin

KW - Chimeric avidin

KW - Ligand binding

KW - NMR

KW - Thermostability

UR - http://www.scopus.com/inward/record.url?scp=84874972758&partnerID=8YFLogxK

U2 - 10.1007/s12104-012-9371-4

DO - 10.1007/s12104-012-9371-4

M3 - Article

VL - 7

SP - 35

EP - 38

JO - BIOMOLECULAR NMR ASSIGNMENTS

JF - BIOMOLECULAR NMR ASSIGNMENTS

SN - 1874-2718

IS - 1

ER -