↓ Skip to main content

Micelle-Induced Folding of Spinach Thylakoid Soluble Phosphoprotein of 9 kDa and Its Functional Implications † , ‡

Overview of attention for article published in Biochemistry, December 2006
Altmetric Badge

Mentioned by

wikipedia
6 Wikipedia pages

Citations

dimensions_citation
15 Dimensions

Readers on

mendeley
27 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Micelle-Induced Folding of Spinach Thylakoid Soluble Phosphoprotein of 9 kDa and Its Functional Implications † , ‡
Published in
Biochemistry, December 2006
DOI 10.1021/bi062148m
Pubmed ID
Authors

Jikui Song, Min S. Lee, Inger Carlberg, Alexander V. Vener, John L. Markley

Abstract

Thylakoid soluble phosphoprotein of 9 kDa (TSP9) has been identified as a plant-specific protein in the photosynthetic thylakoid membrane (Carlberg et al. (2003) Proc. Natl. Acad. Sci. 100, 757-762). Nonphosphorylated TSP9 is associated with the membrane, whereas, after light-induced phosphorylation, a fraction of the phosphorylated TSP9 is released into the aqueous stroma. By NMR spectroscopy, we have determined the structural features of nonphosphorylated TSP9 both in aqueous solution and in membrane mimetic micelles. The results show that both wild type nonphosphorylated TSP9 and a triple-mutant (T46E + T53E + T60E) mimic of the triphosphorylated form of TSP9 are disordered under aqueous conditions, but adopt an ordered conformation in the presence of detergent micelles. The micelle-induced structural features, which are similar in micelles either of SDS or dodecylphosphocholine (DPC), consist of an N-terminal alpha-helix, which may represent the primary site of interaction between TSP9 and binding partners, and a less structured helical turn near the C-terminus. These structured elements contain mainly hydrophobic residues. NMR relaxation data for nonphosphorylated TSP9 in SDS micelles indicated that the molecule is highly flexible with the highest order in the N-terminal alpha-helix. Intermolecular NOE signals, as well as spin probe-induced broadening of NMR signals, demonstrated that the SDS micelles contact both the structured and a portion of the unstructured regions of TSP9, in particular, those containing the three phosphorylation sites (T46, T53, and T60). This interaction may explain the selective dissociation of phosphorylated TSP9 from the membrane. Our study presents a structural model for the role played by the structured and unstructured regions of TSP9 in its membrane association and biological function.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 27 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 4%
Unknown 26 96%

Demographic breakdown

Readers by professional status Count As %
Researcher 8 30%
Professor > Associate Professor 4 15%
Student > Ph. D. Student 4 15%
Student > Master 3 11%
Student > Bachelor 2 7%
Other 1 4%
Unknown 5 19%
Readers by discipline Count As %
Agricultural and Biological Sciences 10 37%
Biochemistry, Genetics and Molecular Biology 5 19%
Computer Science 2 7%
Chemistry 2 7%
Medicine and Dentistry 1 4%
Other 0 0%
Unknown 7 26%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 01 January 2020.
All research outputs
#8,135,326
of 24,397,600 outputs
Outputs from Biochemistry
#7,266
of 22,293 outputs
Outputs of similar age
#43,688
of 162,721 outputs
Outputs of similar age from Biochemistry
#57
of 134 outputs
Altmetric has tracked 24,397,600 research outputs across all sources so far. This one is in the 44th percentile – i.e., 44% of other outputs scored the same or lower than it.
So far Altmetric has tracked 22,293 research outputs from this source. They receive a mean Attention Score of 4.3. This one is in the 17th percentile – i.e., 17% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 162,721 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 16th percentile – i.e., 16% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 134 others from the same source and published within six weeks on either side of this one. This one is in the 7th percentile – i.e., 7% of its contemporaries scored the same or lower than it.