ArticleProtein science : a publication of the Protein Society2007
Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Engineered Chimera Protein Constructs to Facilitate the Production of Heterologous Transmembrane Proteins inInternational journal of molecular sciences · 2024Review
- Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein.Communications biology · 2023Article
- Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.Protein science : a publication of the Protein Society · 2018Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Comparison of the structure and function of phospholamban and the arginine-14 deficient mutant associated with dilated cardiomyopathy.PloS one · 2014Article
- Two different conformations in hepatitis C virus p7 protein account for proton transport and dye release.PloS one · 2014Article
- Article
- An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization.Protein expression and purification · 2012Article
- The small hydrophobic protein of the human respiratory syncytial virus forms pentameric ion channels.The Journal of biological chemistry · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- A systematic assessment of mature MBP in membrane protein production: overexpression, membrane targeting and purification.Protein expression and purification · 2011Article
- Expression and purification of the transmembrane domain of Fukutin-I for biophysical studies.Protein expression and purification · 2010Article
- Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis.The Journal of biological chemistry · 2009Article
- Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles.Biophysical journal · 2009Article
- Expression and purification of isotopically labeled peptide inhibitors and substrates of cAMP-dependant protein kinase A for NMR analysis.Protein expression and purification · 2009Article
- Investigation of the utility of selective methyl protonation for determination of membrane protein structures.Journal of biomolecular NMR · 2008Article
- Construction of a series of vectors for high throughput cloning and expression screening of membrane proteins from Mycobacterium tuberculosis.BMC biotechnology · 2008Article
- Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Biochimica et biophysica acta · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Structural characterization of transmembrane peptides (TMPs) is justified because transmembrane domains of membrane proteins appear to often function independently of the rest of the protein. However, the challenge in obtaining milligrams of isotopically labeled TMPs to study these highly hydrophobic peptides by nuclear magnetic resonance (NMR) is significant. In the present work, a protocol is developed to produce, isotopically label, and purify TMPs in high yield as well as to initially characterize the TMPs with CD and both solution and solid-state NMR. Six TMPs from three integral membrane proteins, CorA, M2, and KdpF, were studied. CorA and KdpF are from Mycobacterium tuberculosis, while M2 is from influenza A virus. Several milligrams of each of these TMPs ranging from 25 to 89 residues were obtained per liter of M9 culture. The initial structural characterization results showed that these peptides were well folded in both detergent micelles and lipid bilayer preparations. The high yield, the simplicity of purification, and the convenient protocol represents a suitable approach for NMR studies and a starting point for characterizing the transmembrane domains of membrane proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.