Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment

Dominique P. Frueh; Haribabu Arthanari; Gerhard Wagner

doi:10.1007/s10858-005-3204-z

Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment

Dominique P. Frueh, Haribabu Arthanari, Gerhard Wagner

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

An experiment that provides a simple procedure to assign backbone nuclei in proteins is presented. The method relies on time-shared evolution of the coherences present in the (HN)NCAHA and (HA)CANNH experiments. By exploiting the fact that some of the coherences are common to both experiments the alpha and amide protons that are simultaneously detected are correlated with each other and with nitrogen and carbon nuclei. Thus, simultaneous assignment of H^α, H^N, C^α and N signals is achieved in a single 3D spectrum. The experiment was tested on the streptococcal protein G B1 domain (GB1) which was easily assigned using a "stairway" procedure and on an 11 kDa domain of the yeast transcriptional co-activator Gal11.

Original language	English (US)
Pages (from-to)	187-196
Number of pages	10
Journal	Journal of Biomolecular NMR
Volume	33
Issue number	3
DOIs	https://doi.org/10.1007/s10858-005-3204-z
State	Published - Nov 2005
Externally published	Yes

Keywords

GB1
Gal11
Nuclear magnetic resonance
Protein backbone assignment
Time-shared

ASJC Scopus subject areas

Biochemistry
Spectroscopy

Access to Document

10.1007/s10858-005-3204-z

Cite this

@article{b379914c909749bd9ba85a4f1fc5e9d2,

title = "Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment",

abstract = "An experiment that provides a simple procedure to assign backbone nuclei in proteins is presented. The method relies on time-shared evolution of the coherences present in the (HN)NCAHA and (HA)CANNH experiments. By exploiting the fact that some of the coherences are common to both experiments the alpha and amide protons that are simultaneously detected are correlated with each other and with nitrogen and carbon nuclei. Thus, simultaneous assignment of Hα, HN, Cα and N signals is achieved in a single 3D spectrum. The experiment was tested on the streptococcal protein G B1 domain (GB1) which was easily assigned using a {"}stairway{"} procedure and on an 11 kDa domain of the yeast transcriptional co-activator Gal11.",

keywords = "GB1, Gal11, Nuclear magnetic resonance, Protein backbone assignment, Time-shared",

author = "Frueh, {Dominique P.} and Haribabu Arthanari and Gerhard Wagner",

note = "Funding Information: We thank Dr. Philipp Selenko for providing the GB1 construct and Anders M. N{\"a}{\"a}r for the gene of the Gal11 domain. This research was supported by NIH (grants GM 47467 and RR 00995).",

year = "2005",

month = nov,

doi = "10.1007/s10858-005-3204-z",

language = "English (US)",

volume = "33",

pages = "187--196",

journal = "Journal of Biomolecular NMR",

issn = "0925-2738",

publisher = "Springer Netherlands",

number = "3",

}

TY - JOUR

T1 - Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment

AU - Frueh, Dominique P.

AU - Arthanari, Haribabu

AU - Wagner, Gerhard

N1 - Funding Information: We thank Dr. Philipp Selenko for providing the GB1 construct and Anders M. Näär for the gene of the Gal11 domain. This research was supported by NIH (grants GM 47467 and RR 00995).

PY - 2005/11

Y1 - 2005/11

N2 - An experiment that provides a simple procedure to assign backbone nuclei in proteins is presented. The method relies on time-shared evolution of the coherences present in the (HN)NCAHA and (HA)CANNH experiments. By exploiting the fact that some of the coherences are common to both experiments the alpha and amide protons that are simultaneously detected are correlated with each other and with nitrogen and carbon nuclei. Thus, simultaneous assignment of Hα, HN, Cα and N signals is achieved in a single 3D spectrum. The experiment was tested on the streptococcal protein G B1 domain (GB1) which was easily assigned using a "stairway" procedure and on an 11 kDa domain of the yeast transcriptional co-activator Gal11.

AB - An experiment that provides a simple procedure to assign backbone nuclei in proteins is presented. The method relies on time-shared evolution of the coherences present in the (HN)NCAHA and (HA)CANNH experiments. By exploiting the fact that some of the coherences are common to both experiments the alpha and amide protons that are simultaneously detected are correlated with each other and with nitrogen and carbon nuclei. Thus, simultaneous assignment of Hα, HN, Cα and N signals is achieved in a single 3D spectrum. The experiment was tested on the streptococcal protein G B1 domain (GB1) which was easily assigned using a "stairway" procedure and on an 11 kDa domain of the yeast transcriptional co-activator Gal11.

KW - GB1

KW - Gal11

KW - Nuclear magnetic resonance

KW - Protein backbone assignment

KW - Time-shared

UR - http://www.scopus.com/inward/record.url?scp=31444432912&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=31444432912&partnerID=8YFLogxK

U2 - 10.1007/s10858-005-3204-z

DO - 10.1007/s10858-005-3204-z

M3 - Article

C2 - 16331423

AN - SCOPUS:31444432912

SN - 0925-2738

VL - 33

SP - 187

EP - 196

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 3

ER -

Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this