Structure and dynamics of the Pf1 filamentous bacteriophage coat protein in micelles.
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Summary
The combination of results from 1H/15N heteron nuclear correlation, 1H homonuclear correlation, and 1H Homonuclear Overhauser effect experiments assigns the resonances to specific residues and demonstrates that residues 30-40 of the coat protein have a helical secondary structure.
- Type
- article
- Published
- 1987-03-10
- Cited by
- 49
- References
- 43
- OpenAlex
- https://openalex.org/W1983316882
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:27359882
Keywords
Citation, Altmetrics, Icon, Social media, Fake news
References
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- First observation of amino acid side chain dynamics in membrane proteins using high field deuterium nuclear magnetic resonance spectroscopy.
- Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation
- Three-dimensional structure of orthorhombic purple membrane at 6.5 A resolution.
- Distortionless enhancement of NMR signals by polarization transfer
- Dynamics of a hydrophobic peptide in membrane bilayers by solid-state nuclear magnetic resonance.
- Evidence for a major conformational change of coat protein in assembly of fl bacteriophage
- Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein.
- Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.
- An improved method for heteronuclear chemical shift correlation by two-dimensional NMR
- Association of newly synthesized major f1 coat protein with infected host cell inner membrane.
- Structure and Dynamics of FD Coat Protein.
- A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆
- Structural properties of fd coat protein in sodium dodecyl sulfate micelles.
- 19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles.
- Two‐dimensional spectroscopy. Application to nuclear magnetic resonance
- Computed circular dichroism spectra for the evaluation of protein conformation.
Cited by
- Detergent-solubilized M13 coat protein exists as an asymmetric dimer. Observation of individual monomers by 15N, 13C and 1H nuclear magnetic resonance spectroscopy.
- NMR of Proteins and Small Biomolecules
- Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance.
- Neutron diffraction studies of the structure of filamentous bacteriophage Pf1. Demonstration that the coat protein consists of a pair of alpha-helices with an intervening, non-helical surface loop.
- Structure and dynamics of a membrane protein in micelles from three solution NMR experiments
- Contemporary methods in structure determination of membrane proteins by solution NMR.
- Comparison of the dynamics of the membrane‐bound form of fd coat protein in micelles and in bilayers by solution and solid‐state nitrogen‐15 nuclear magnetic resonance spectroscopy
- Secondary structure of filamentous bacteriophage coat protein is preserved in lipid environments.
- Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly.
- Resolution and measurement of heteronuclear dipolar couplings of a noncrystalline protein immobilized in a biological supramolecular assembly by proton-detected MAS solid-state NMR spectroscopy
- Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
- Nitrogen-15 NMR spectroscopy of proteins in solution
- Detection of 1H homonuclear NOE between amide sites in proteins with 1H15N heteronuclear correlation spectroscopy
- Solution- and solid-state NMR studies of GPCRs and their ligands.
- Observation of labile amide protons via indirect detection of 15N single-quantum transitions
- Simulation of a sodium dodecylsulfate micelle in aqueous solution
- Determination of the structure of a membrane-incorporated ion channel. Solid-state nuclear magnetic resonance studies of gramicidin A.
- A light-harvesting antenna protein retains its folded conformation in the absence of protein-lipid and protein-pigment interactions.
- Proton NMR conformational study of an annexin I fragment: influence of a phospholipidic micellar environment.
- Detection of a structural interconversion in a peptide in solution with sensitivity-enhanced 15N chemical-exchange NMR spectroscopy
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