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Article

Site-directed spin-labeling study of the light-harvesting complex CP29.

Biophysical journal - 6 May 2009

Kavalenka Aleh A, Spruijt Ruud B, Wolfs Cor J A M, Strancar Janez, Croce Roberta, Hemminga Marcus A, van Amerongen Herbert

Abstract excerpt

The topology of the long N-terminal domain (approximately 100 amino-acid residues) of the photosynthetic Lhc CP29 was studied using electron spin resonance. Wild-type protein containing a single cysteine at position 108 and nine single-cysteine mutants were produced, allowing to label different parts of the domain with a nitroxide spin label. In all cases, the apoproteins were either solubilized in detergent or...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19413967
DOI: 10.1016/j.bpj.2009.01.038
PMCID: PMC2711397

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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