| Title |
NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution
|
|---|---|
| Published in |
Journal of Biomolecular NMR, October 2002
|
| DOI | 10.1023/a:1020902915969 |
| Pubmed ID | |
| Authors |
August Andersson, Lena Mäler |
| Abstract |
The structure and dynamics of the gastrointestinal peptide hormone motilin, consisting of 22 amino acid residues, have been studied in the presence of isotropic q = 0.5 phospholipid bicelles. The NMR solution structure of the peptide in acidic bicelle solution was determined from 203 NOE-derived distance constraints and six backbone torsion angle constraints. Dynamic properties for the 13Calpha-1H vector in Leu10 were determined for motilin specifically labeled with 13C at this position by analysis of multiple-field relaxation data. The structure reveals an ordered alpha-helical conformation between Glu9 and Lys20. The N-terminus is also well structured with a turn resembling that of a classical beta-turn. The 13C dynamics clearly show that motilin tumbles slowly in solution, with a correlation time characteristic of a large object. It was also found that motilin has a large degree of local flexibility as compared with what has previously been reported in SDS micelles. The results show that motilin interacts with the bicelle, displaying motional properties of a peptide bound to a membrane. In comparison, motilin in neutral bicelles seems less structured and more flexible. This study shows that the small isotropic bicelles are well suited for use as membrane-mimetic for structural as well as dynamical investigations of membrane-bound peptides by high-resolution NMR. |
Mendeley readers
The data shown below were compiled from readership statistics for 30 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 2 | 7% |
| Germany | 1 | 3% |
| Unknown | 27 | 90% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 11 | 37% |
| Professor | 4 | 13% |
| Student > Master | 4 | 13% |
| Student > Ph. D. Student | 3 | 10% |
| Professor > Associate Professor | 3 | 10% |
| Other | 2 | 7% |
| Unknown | 3 | 10% |
| Readers by discipline | Count | As % |
|---|---|---|
| Chemistry | 9 | 30% |
| Agricultural and Biological Sciences | 9 | 30% |
| Biochemistry, Genetics and Molecular Biology | 7 | 23% |
| Psychology | 1 | 3% |
| Materials Science | 1 | 3% |
| Other | 0 | 0% |
| Unknown | 3 | 10% |
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 20 July 2018.
All research outputs
#8,535,472
of 25,374,647 outputs
Outputs from Journal of Biomolecular NMR
#140
of 561 outputs
Outputs of similar age
#17,269
of 49,679 outputs
Outputs of similar age from Journal of Biomolecular NMR
#2
of 5 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 561 research outputs from this source. They receive a mean Attention Score of 3.2. This one is in the 43rd percentile – i.e., 43% of its peers scored the same or lower than it.
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