H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide

Piotr Wysoczanski; Robert J. Mart; E. Joel Loveridge; Christopher Williams; Sara B. -M. Whittaker; Matthew P. Crump; Rudolf K. Allemann

doi:10.1007/s12104-012-9407-9

H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide

Piotr Wysoczanski, Robert J. Mart, E. Joel Loveridge, Christopher Williams, Sara B. -M. Whittaker, Matthew P. Crump, Rudolf K. Allemann^*

^*Corresponding author for this work

Research output: Contribution to journal › Article (Academic Journal) › peer-review

1 Citation (Scopus)

Abstract

Here we report the H-1, C-13 and N-15 resonance assignments of free Bcl-x(L) and of Bcl-x(L) in complex with an azobenzene-modified peptide derived from the BH3 domain of the pro-apoptotic Bak. The spectra suggest predominantly folded proteins; chemical shift difference analysis provides a detailed view of the reorganization occurring on peptide binding.

Original language	English
Article number	10.1007/s12104-012-9378-x
Pages (from-to)	187-191
Number of pages	5
Journal	Biomolecular NMR Assignments
Volume	7
Issue number	2
DOIs	https://doi.org/10.1007/s12104-012-9407-9
Publication status	Published - Oct 2013

Research Groups and Themes

Bristol BioDesign Institute
Organic & Biological

Keywords

Bcl-2 family
synthetic biology
Azobenzene
BCL-X-L
APOPTOSIS
Photonano-switches
PROTEIN
Bcl-x(L)

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Wysoczanski, P., Mart, R. J., Loveridge, E. J., Williams, C., Whittaker, S. B. .-M., Crump, M. P., & Allemann, R. K. (2013). H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide. Biomolecular NMR Assignments, 7(2), 187-191. Article 10.1007/s12104-012-9378-x. https://doi.org/10.1007/s12104-012-9407-9

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title = "H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide",

abstract = "Here we report the H-1, C-13 and N-15 resonance assignments of free Bcl-x(L) and of Bcl-x(L) in complex with an azobenzene-modified peptide derived from the BH3 domain of the pro-apoptotic Bak. The spectra suggest predominantly folded proteins; chemical shift difference analysis provides a detailed view of the reorganization occurring on peptide binding.",

keywords = "Bcl-2 family, synthetic biology, Azobenzene, BCL-X-L, APOPTOSIS, Photonano-switches, PROTEIN, Bcl-x(L)",

author = "Piotr Wysoczanski and Mart, \{Robert J.\} and Loveridge, \{E. Joel\} and Christopher Williams and Whittaker, \{Sara B. -M.\} and Crump, \{Matthew P.\} and Allemann, \{Rudolf K.\}",

year = "2013",

month = oct,

doi = "10.1007/s12104-012-9407-9",

language = "English",

volume = "7",

pages = "187--191",

journal = "Biomolecular NMR Assignments",

issn = "1874-2718",

publisher = "Springer Science and Business Media B.V.",

number = "2",

}

H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide. / Wysoczanski, Piotr; Mart, Robert J.; Loveridge, E. Joel et al.
In: Biomolecular NMR Assignments, Vol. 7, No. 2, 10.1007/s12104-012-9378-x, 10.2013, p. 187-191.

Research output: Contribution to journal › Article (Academic Journal) › peer-review

TY - JOUR

T1 - H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide

AU - Wysoczanski, Piotr

AU - Mart, Robert J.

AU - Loveridge, E. Joel

AU - Williams, Christopher

AU - Whittaker, Sara B. -M.

AU - Crump, Matthew P.

AU - Allemann, Rudolf K.

PY - 2013/10

Y1 - 2013/10

N2 - Here we report the H-1, C-13 and N-15 resonance assignments of free Bcl-x(L) and of Bcl-x(L) in complex with an azobenzene-modified peptide derived from the BH3 domain of the pro-apoptotic Bak. The spectra suggest predominantly folded proteins; chemical shift difference analysis provides a detailed view of the reorganization occurring on peptide binding.

AB - Here we report the H-1, C-13 and N-15 resonance assignments of free Bcl-x(L) and of Bcl-x(L) in complex with an azobenzene-modified peptide derived from the BH3 domain of the pro-apoptotic Bak. The spectra suggest predominantly folded proteins; chemical shift difference analysis provides a detailed view of the reorganization occurring on peptide binding.

KW - Bcl-2 family

KW - synthetic biology

KW - Azobenzene

KW - BCL-X-L

KW - APOPTOSIS

KW - Photonano-switches

KW - PROTEIN

KW - Bcl-x(L)

U2 - 10.1007/s12104-012-9407-9

DO - 10.1007/s12104-012-9407-9

M3 - Article (Academic Journal)

C2 - 22744789

SN - 1874-2718

VL - 7

SP - 187

EP - 191

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

M1 - 10.1007/s12104-012-9378-x

ER -

H-1, C-13 and N-15 chemical shift assignments of unliganded Bcl-x(L) and its complex with a photoresponsive Bak-derived peptide

Abstract

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Keywords

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