Pith. sign in

REVIEW 1 major objections 5 minor 38 references

Neutron Reflectometry Reveals Conformational Changes in a Mechanosensitive Protein Induced by an Antimicrobial Peptide in Tethered Lipid Bilayers

T0 review · 1 major / 5 minor · reviewed 2026-08-15 · deepseek-v4-flash

Challenge this review Re-run · record.json Download PDF Read on arXiv ↗ Review JSON

Pith's one-line read Pexiganan shortens the C-terminal protrusion of the mechanosensitive channel MscL by about 8 Å, the first direct evidence that an antimicrobial peptide triggers a gating-like conformational change.

desk verdict Promising new tethered-bilayer PNR platform shows a real 46-to-38 Å protrusion change in MscL on pexiganan, but the peptide is left out of the model, so the attribution to a protein conformational change needs one more control. read the letter →

arxiv 2506.16972 v1 pith:HHY3L5J5 submitted 2025-06-20 physics.bio-ph

Sophie E. Ayscough , Maximilian W. A. Skoda , James Doutch , Andrew Caruana , Christy Kinane , Luke Clifton , Simon Titmuss This is my paper · ORCID
classification physics.bio-ph
keywords MscLmechanosensitiveionchannelantimicrobialpeptidepexigananneutronreflectometrytetheredlipidbilayercell-freeproteinexpressionsmall-anglescattering
verification ladder T0 review T1 audit T2 compute T3 formal

The pith

A machine-rendered reading of the paper's core claim, the machinery that carries it, and where it could break.

The reading

This paper seeks to establish that the antimicrobial peptide pexiganan does more than perturb the lipid bilayer: it triggers a conformational change in the mechanosensitive ion channel MscL, the bacterial pressure-relief valve. Using polarized neutron reflectivity on a polymer-tethered lipid bilayer containing cell-free expressed MscL, the authors measure the solvent-facing C-terminal protrusion of the channel shrinking from 46 ± 3 Å to 38 ± 3 Å after exposure to 1.6 µM pexiganan and remaining near 38 Å at 3.2 µM. They argue that this shortening matches the retraction of the C-terminus into the transmembrane domain predicted for channel opening, and they support the assignment with small-angle neutron scattering on MscL vesicles showing a comparable radius-of-gyration increase. A sympathetic reader would care because it offers a structural mechanism by which antimicrobial peptides could kill bacteria by gating open an ion channel, at concentrations below those needed for wholesale membrane disruption.

What carries the argument

The load-bearing measurement is polarized neutron reflectivity (PNR) from a polymer-tethered bilayer, modelled as a stack of slabs from the silicon substrate out to solution: oxide, permalloy, gold, PDP anchor, PEG brush, inner and outer lipid leaflets, and a final slab representing the MscL protrusion. The lipid leaflets are parametrized by area per molecule and water molecules per lipid head, the transmembrane protein enters as a volume fraction, and the protrusion slab has its own fitted thickness; Bayesian posterior sampling is used to estimate parameter uncertainties and to show that the protrusion-thickness posterior shifts after pexiganan addition. Supporting characterization comes from small-angle neutron scattering of MscL-containing vesicles, where a two-level Guinier-Porod fit yields a protein radius of gyration of 26–29 Å, matching the crystal structure of individual MscL channels and indicating that the channels are incorporated as unclustered monomers rather than large aggregates.

What would settle it

A protein-free POPC:POPG tethered bilayer measured by polarized neutron reflectivity before and after 1.6 µM pexiganan would settle the point: if the apparent protrusion-layer thickness or scattering length density changes by roughly the same 8 Å, the MscL conformational assignment is not supported. A complementary check is patch-clamp recording of MscL proteoliposomes at 1.6 µM pexiganan, which should show channel opening if the structural change is gating.

Watch

Extended reading notes

Core claim

The central claim is that pexiganan induces a conformational change in MscL that appears as a decrease in the fitted thickness of the channel's C-terminus-containing protrusion in a tethered lipid bilayer: from 46 ± 3 Å in the pristine bilayer to 38 ± 3 Å at 1.6 µM and 38 ± 5 Å at 3.2 µM pexiganan, with the Bayesian posterior for this parameter shifting to lower values. The accompanying changes, protein coverage falling from 14% to 9–11% and bilayer coverage rising from 0.66 to 0.71–0.73, are shown by the authors to be the expected signature of open channels occluding a larger area than closed channels. The authors present this as the first direct experimental evidence of an antimicrobial peptide triggering a structural change in the C-terminus of MscL, consistent with a gating motion previously predicted by molecular dynamics and inferred from EPR and FRET measurements.

Load-bearing premise

The load-bearing assumption is that the fitted protrusion thickness decrease is caused by protein movement, not by pexiganan's own scattering contribution, since pexiganan is not included in the reflectivity model and the paper reports no protein-free bilayer-plus-pexiganan control.

Editorial extensions

If this is right

  • If the protrusion shortening is genuine, PNR on tethered bilayers provides a direct structural readout of MscL gating that does not require detergents or protein clustering.
  • The correlated rise in bilayer coverage and fall in protein coverage can serve as a secondary fingerprint of channel opening in future screens of antimicrobial peptides.
  • The result places a structural constraint on models of MscL gating: the C-terminus retracts by roughly 8 Å toward the transmembrane domain rather than moving outward.
  • Because the change saturates between 1.6 and 3.2 µM pexiganan, the effect occurs at the lower end of reported minimum inhibitory concentrations, suggesting channel gating precedes membrane disruption.
  • The same tethered-bilayer platform can be applied to other amphipathic drugs and MscL mutants to test whether gating-like conformational changes are a general antimicrobial-peptide mechanism.

Reading between the lines

Editorial extensions of the paper, not claims the author makes directly.

  • Beyond the paper: if pexiganan gates MscL open at sub-MIC concentrations, combination therapies pairing antimicrobial peptides with antibiotics that enter through the MscL pore, such as streptomycin-like aminoglycosides, should show synergistic killing; this is testable in bacterial viability assays.
  • Beyond the paper: the protrusion thickness being 38 Å at both 1.6 and 3.2 µM pexiganan suggests a two-state transition rather than a graded response, and patch-clamp recordings at intermediate concentrations would reveal whether the structural change is all-or-none.
  • Beyond the paper: because pexiganan is absent from the reflectivity model, a protein-free bilayer control exposed to pexiganan would determine how much of the apparent protrusion change is peptide contrast; without that control, the quantitative 8 Å number is tied to the model's assumption.
  • Beyond the paper: using deuterated pexiganan would change the peptide's scattering length density and allow the peptide's own location to be fitted rather than omitted, providing a direct test of where the peptide acts.
Share X Bluesky LinkedIn Reddit HN

Signed reviews

No signed human review yet.

Editorial analysis

A structured set of objections, weighed in public.

Desk editor's note, referee report, and a circularity audit.

Referee Report

1 major / 5 minor

Summary. The manuscript reports a cell-free, detergent-free expression of the mechanosensitive channel MscL into POPC:POPG vesicles, SANS characterization of the vesicle-embedded protein (Rg = 26-29 Å), formation of PEG-tethered lipid bilayers on gold, and polarized neutron reflectivity (PNR) analysis of the bilayer before and after exposure to the antimicrobial peptide pexiganan. The fitted thickness of the MscL protrusion decreases from 46 ± 3 Å to 38 ± 3 Å at 1.6 μM pexiganan and to 38 ± 5 Å at 3.2 μM (Table II), with a shifted posterior distribution (Fig. 7). The authors interpret this as the first direct experimental evidence of an AMP-induced conformational change in the C-terminal protrusion of MscL, consistent with channel gating.

Significance. If the attribution holds, this is a valuable structural observation linking antimicrobial-peptide action to MscL gating, with potential implications for antibiotic mechanisms and drug design. The experimental platform is a genuine advance: cell-free expression avoids detergents, the polymeric tether provides a flexible membrane mimetic, and the PNR analysis uses three solvent contrasts and two spin contrasts with Bayesian posterior sampling. The authors provide the fitting code and data repository, which strengthens reproducibility. The two peptide concentrations give consistent thickness values, and the model selection for protrusion orientation is based on log-evidence. However, the central interpretation rests on an unvalidated assumption that pexiganan contributes negligibly to the reflectivity; the reported 'direct experimental evidence' is therefore not yet secured.

major comments (1)
  1. [Section II.G and SI Section 2] The central claim—that the 46-to-38 Å protrusion decrease reflects an MscL conformational change—relies on a model in which pexiganan is not explicitly included. As stated in Section II.G and SI Section 2: 'Pexiganan is not explicitly included in the model.' Pexiganan is an amphipathic cationic peptide known to insert at the lipid headgroup/tail interface (ref. 9), and after the buffer rinse it will remain in the bilayer. This peptide contributes to the scattering length density in the very layers (outer headgroup and protrusion region) whose thickness and SLD are being fitted. Because the model contains no peptide component, all post-peptide SLD changes are absorbed into the MscL protrusion thickness, the protein coverage, and the bilayer coverage parameters. A thin peptide-rich layer at the outer leaflet or at the base of the protrusion could plausibly mimic a reduced protrusion thickness. The justification for omitting the peptide is a prior thesis measurement (ref. 46) rather than a measurement in the present tethered-bilayer system, and no protein-free POPC:POPG tethered bilayer challenged with pexiganan is reported. To secure the attribution, the authors should either (i) add an explicit pexiganan layer to the model with the peptide:lipid ratio constrained by an independent assay, or (ii) measure a protein-free control bilayer under the same pexiganan challenge. Without one of these, the claim of 'first direct experimental evidence' is overstated.
minor comments (5)
  1. [SI Section 2B and Table II] The argument that the increase in bilayer coverage from 0.66 to 0.73 is 'a signature of channel opening' is a consistency check rather than an independent prediction: the predicted value of 0.72 is derived from the fitted pre-peptide protein coverage (13.7%) and an assumed open-channel radius of 35 Å, while the post-peptide protein coverage is itself a fitted parameter that decreases to 9-11%. This supporting evidence should be rephrased as model-dependent consistency, not as confirmation.
  2. [Section III.D] The PNR experiment was performed on a single bilayer preparation. The agreement between the 1.6 and 3.2 μM pexiganan concentrations is encouraging, but an independent bilayer replicate would strengthen the generality of the reported 8 Å protrusion decrease.
  3. [SI Section 2 (Python code, sum_mscl)] The protein scattering length density depends on assumed H/D exchange fractions (0.7 for the transmembrane region and 0.9 for the cytoplasmic region). The authors do not report a sensitivity analysis of these values; a brief test over a plausible range would clarify how robust the fitted protrusion thickness and its peptide-induced shift are to this assumption.
  4. [SI Section 5B] The SANS experiments with pexiganan show a 62.5% decrease in scattered intensity and creaming of lipid/protein, indicating vesicle destabilization. The authors should discuss whether analogous peptide-induced effects on the tethered bilayer could influence the fitted bilayer coverage or roughness parameters in the PNR analysis.
  5. [Throughout] A few typographical errors should be corrected, including 'deterimental' in the Introduction and 'Bicinchronic acid' in SI Section 4 (should be 'bicinchoninic acid').

Circularity Check

0 steps flagged · score 0.0 of 10

No circularity: the protrusion thickness is a directly fitted PNR parameter, and the SI coverage calculation is an independent prediction, not an input to the post-peptide fit.

full rationale

The paper's central claim is that the fitted MscL protrusion thickness decreases from 46 ± 3 Å to 38 ± 3 Å / 38 ± 5 Å after pexiganan addition (Table II), with the posterior shift in Fig. 7. This quantity is a free parameter of the reflectivity model, optimized against the measured reflectivity; it is not derived from the model inputs or from the hypothesis that pexiganan gates MscL. The SI Section 2B 'Justification of observed variation in bilayer coverage' combines pre-peptide fitted bilayer coverage (0.66) and protein coverage (0.137) with assumed open-channel dimensions from the literature to predict a post-gating coverage of 0.72, and then compares this with the independently fitted post-peptide value of 0.73. That is a genuine prediction from separate inputs, not an equation that reproduces the fitted value by construction. The model's omission of pexiganan is justified by a prior thesis measurement of a low peptide:lipid ratio (ref 46); this is an external empirical input rather than a self-referential derivation, and it does not make the central structural result equivalent to an input. No uniqueness theorem from the same authors is invoked, and no known result is merely renamed. While the absence of a protein-free peptide control and the single-bilayer replication are legitimate scientific concerns, they are correctness or robustness issues, not circularity. Therefore the paper contains no significant circular step.

Assumptions & free parameters 5 free parameters · 7 assumptions · 0 invented entities

The central fit depends on several modeling choices: the single-slab description of the C-terminal protrusion, the exclusion of pexiganan from the SLD calculation, assumed H/D exchange fractions in the protein scattering length, and geometric dimensions for the open channel taken from the literature. None of these are derived in the paper; they are inputs. There are no invented physical entities.

free parameters (5)
  • MscL protrusion thickness = 46 ± 3 Å; 38 ± 3 Å (1.6 μM PXG); 38 ± 5 Å (3.2 μM PXG)
    The central fitted observable; the paper interprets its 8 Å decrease as C-terminal conformational change (Table II).
  • Protein coverage in the transmembrane region = 0.14 ± 0.01; 0.09 ± 0.01; 0.11 ± 0.01
    Fitted volume fraction of MscL in the bilayer; its decrease is used to support the gating interpretation (Table II).
  • Bilayer coverage = 0.66 ± 0.02; 0.73 ± 0.02; 0.71 ± 0.02
    Fitted fraction of the footprint covered by bilayer; its increase is predicted and then used as a gating signature (Table II, SI 2B).
  • H/D exchange fraction in protein SLD = 0.7 (transmembrane), 0.9 (cytoplasmic)
    Chosen values in the SLD calculation (SI Section 6); they set the protein and protrusion SLDs and therefore affect the fitted thickness.
  • Lipid area per molecule (inner/outer leaflet) and waters per lipid head = 79/98 to 99 Ų; 6 WPLH
    Fitted in the PNR model; the larger-than-usual APM supports the claim that the bilayer is under tension (Table II).
assumptions (7)
  • standard math Optical matrix formalism and Nevot-Croce roughness describe the reflectivity of the layered interface.
    Used in Section II.G and the RefNX implementation (SI Section 6) to compute reflectivity from the layer model; a background method, not derived here.
  • domain assumption Scattering length densities are volume-fraction averages of components with literature molecular volumes and atomic scattering lengths.
    SI Section 2; lipid head/tail volumes from RefNX and cited literature are needed to convert APM/WPLH fits into SLD profiles.
  • ad hoc to paper The C-terminal protrusion of MscL is represented as a single homogeneous slab whose volume fraction derives from crystal-structure volume ratios.
    SI Sections 2 and 6 (Ccoverage calculation); this simplified geometric description is what the fitted 46 to 38 Å change is attributed to.
  • ad hoc to paper Pexiganan contributes negligibly to the layer scattering length density and is excluded from the model.
    Section II.G and SI Section 2; justified by a prior thesis peptide:lipid measurement (ref 46), not by an assay in this system.
  • ad hoc to paper The H/D exchange fractions used in the protein scattering length (0.7 transmembrane, 0.9 cytoplasmic regions) are correct.
    SI Section 6 code (sum mscl, sum mscl cterminal); these values set the protein SLD and hence the fitted protrusion coverage and thickness.
  • domain assumption The open-state channel geometry (radius increasing from 25 to 35 Å, C-terminus retraction) from the Perozo/Bavi literature is used to predict bilayer coverage changes on gating.
    SI Section 2B; the coverage prediction (0.72) and its agreement with the fitted 0.73 are used to support channel opening.
  • domain assumption A two-level Guinier-Porod model can separate vesicle-level and protein-level SANS contributions with a fixed vesicle Rg.
    SI Section 5; the protein Rg (26 to 29 Å) is the second level of a fit where the vesicle level has fixed Rg 106 Å.

how reviews work

0 comments
Cite this review

Pith. "Pith review of Neutron Reflectometry Reveals Conformational Changes in a Mechanosensitive Protein Induced by an Antimicrobial Peptide in Tethered Lipid Bilayers." pith.science (2026). https://pith.science/paper/HHY3L5J5

@misc{pith2026250616972,
  author       = {Pith},
  title        = {Pith review of: Neutron Reflectometry Reveals Conformational Changes in a Mechanosensitive Protein Induced by an Antimicrobial Peptide in Tethered Lipid Bilayers},
  year         = {2026},
  howpublished = {\url{https://pith.science/paper/HHY3L5J5}},
  note         = {Machine review of arXiv:2506.16972}
}
abstract

Membrane proteins serve a wide range of vital roles in the functioning of living organisms. Compared to other classes of proteins, determining membrane protein structures remains a challenge, in large part due to the difficulty in establishing experimental conditions that can preserve the correct conformation and function of the protein in isolation from its native environment. We investigated the ion channel in lipid vesicles and in a planar lipid bilayer. By using a polymeric tether our planar membrane mimetic was not constrained by the underlying solid substrate, making it sufficiently flexible to allow for increases in bilayer curvature and changes in membrane tension. We used quartz crystal microbalance with dissipation (QCM-D), and polarised neutron reflectivity (PNR) to show the formation of MscL containing phospholipid bilayers, tethered with a high density PEG layer onto gold substrates from vesicle rupture. The MscL containing vesicles were separately characterised with small angle neutron scattering (SANS). MscL was expressed into vesicles using cell free protein expression. Analysing these vesicles with small angle neutron scattering, the radius of gyration of the protein was determined to be between 26-29~\AA{}, consistent with the crystal structure of individual MscL channels. The MscL composition of the formed bilayer was 14\%$v/v$, close to the initial composition of the vesicles, and a protein protrusion extending ca. 46~\AA{} into the solvent was determined by PNR. Addition of 1.6 and 3.2 $\mu$M pexiganan resulted in a decrease in the protrusion of MscL (from $\sim$46 to $\sim$38~\AA{}). To our knowledge, these findings represent the first direct experimental evidence of a structural change in the C-terminus containing protrusion of MscL, triggered by an antimicrobial peptide.

Figures

Figures reproduced from arXiv: 2506.16972 by the authors.

Figure 1
Figure 1. FIG. 1. Small angle neutron scattering (SANS) of MscL [PITH_FULL_IMAGE:figures/full_fig_p005_1.png] view at source ↗
Figure 4
Figure 4. Bilayer formation by rupture of the MscL containing vesicles incorporates the DSPE part of the tether into the inner leaflet of the bilayer and so the tethered bilayer model does not have a distinct DSPE layer. For the two lipid leaflets of the lipid bilayer, separate area per molecule (APM) and water per lipid heads (WPLH) parameters were fitted. The best fit APM values for the inner and outer lipid bilayer leaflet… view at source ↗
Figure 2
Figure 2. FIG. 2. Fitted neutron reflectivity of PDP-PEG2000-DSPE tethered [PITH_FULL_IMAGE:figures/full_fig_p007_2.png] view at source ↗
Figures from the paper (5 more)
Figure 3
Figure 3. Figure 3: FIG. 3. QCM-D measurement of the changes in (3rd Overtone) Freque [PITH_FULL_IMAGE:figures/full_fig_p008_3.png]
Figure 4
Figure 4. Figure 4: FIG. 4. Fitted neutron reflectivity of PDP-PEG2000-DSPE tethered [PITH_FULL_IMAGE:figures/full_fig_p009_4.png]
Figure 5
Figure 5. Figure 5: FIG. 5. Fitted Reflectivity profiles of tethered bilayers contai [PITH_FULL_IMAGE:figures/full_fig_p010_5.png]
Figure 6
Figure 6. Figure 6: FIG. 6. Fitted Reflectivity profiles of tethered bilayers contai [PITH_FULL_IMAGE:figures/full_fig_p011_6.png]
Figure 7
Figure 7. Figure 7: FIG. 7. Posterior distributions of the MscL protrusion thick [PITH_FULL_IMAGE:figures/full_fig_p012_7.png]

Discussion (0). Continue with ORCID to comment.

Reference graph

Works this paper leans on

38 extracted references · 37 canonical work pages

  1. [1]

    QUAR TZ-CR YST AL MICROBALANCE WITH DISSIPA TION (QCM-D) A typical QCM-D protocol followed the following steps:

    work page

  2. [2]

    After testing that the frequency is stable for 30 min with on ly clean buffer in the cell, i.e. there is no desorption of tether occurring, adsorption of contaminants or bubbles in the system, then a solution of vesicles was passed through the cells at 1 mL/min using the peristaltic pump. 10 ml of vesicle solution is pass ed through each QCM cell

    work page

  3. [3]

    Buffer solution (10 mL) was passed through each of the flow cells and the measurement started with the sensors in HEPES buffer

    work page

  4. [4]

    Since tethered bilayers are viscoelastic it was inappropriate to analyse the results quanti- tatively using the Sauerbrey equation

    This was immediately followed by a salt rupture step, push ing 5 mL of lower salt concentration 150 mM NaCl HEPES buffer through the QCM cell. Since tethered bilayers are viscoelastic it was inappropriate to analyse the results quanti- tatively using the Sauerbrey equation. The system has high water content in the tether layer and also in any tethered vesi...

    work page

  5. [5]

    After 1 h, 300 mM NaCl HEPES buffer was passed through the cells t o remove excess vesicles

    work page

  6. [6]

    Python code for fitting polarized neutron reflectivity data measured from the tethered bilayer in three sub-phase contrasts

    REFLECTIVITY MODEL IMPLEMENTED IN PYTHON USING REFNX Listing 1. Python code for fitting polarized neutron reflectivity data measured from the tethered bilayer in three sub-phase contrasts. The full set of Jupyter note books used for the analysis of PNR can be found in the data repository for the manuscript [27]. #! / u s r / b i n / env p y t h o n # c o d ...

    work page 1990

  7. [7]

    Values for the lipid head and tail group volumes were taken from the RefNX database[7–9] The SLDs of the silicon and silicon oxide were fixed at literat ure values

    NEUTRON REFLECTIVITY DA T A ANAL YSIS While the layers from silicon oxide to poly(ethylene glycol) (PEG2000) were parame- terised as simple slabs, the DSPE and lipid bilayer were para meterised in terms of area per molecule (APM) and water molecules per lipid head (WPLH) using l iterature values for molecular volumes and atomic scattering lengths.[3–6] Th...

    work page

  8. [8]

    The Bayesian approach is useful for examining parameter covariances

    ERROR ANAL YSIS POSTERIOR DISTRIBUTIONS RefNX uses a Bayesian approach employing a Markov-chain Mont e Carlo algorithm to investigate the posterior probability distribution of the model parameters. The Bayesian approach is useful for examining parameter covariances. The figures below (Figs. S2, S3 and S4) show the corner plots for the conditions without PX...

    work page

Show all 38 references
  1. [9]

    13.5 mg of POPC and 4.5 mg of POPC were dissolved in the minimum amount of chlo- roform and the chloroform removed under a stream of nitrogen to produce a dried lipid film

    CELL-FREE PROTEIN EXPRESSION First a concentrated solution (18 mg/mL) of 3:1 POPC:POPG lip ids was prepared. 13.5 mg of POPC and 4.5 mg of POPC were dissolved in the minimum amount of chlo- roform and the chloroform removed under a stream of nitrogen to produce a dried lipid fi...

  2. [10]

    SMALL ANGLE NEUTRON SCA TTERING ANAL YSIS Hammouda et al. proposed a generalized Guinier-Porod approach to fitting the scattering from a mixture of arbitrary shapes or fractal structures for which it is difficult to build analytical models.[15] For each particulate type in the sy...

  3. [11]

    coli HY Kit — leap and lead — biotec hrab- bit.com, https://www.biotechrabbit.com/rts-500-proteomaster-e-coli-hy-kit-405

    biotechrabbit — RTS 500 ProteoMaster E. coli HY Kit — leap and lead — biotec hrab- bit.com, https://www.biotechrabbit.com/rts-500-proteomaster-e-coli-hy-kit-405. html, [Accessed 15-Aug-2024] (2023)

    2023

  4. [12]

    F. Inci, U. Celik, B. Turken, H. ¨Ozg¨ ur¨Ozer, F. N. Kok, Construction of p-glycoprotein incorporated tethered lipid bilayer membranes, Biochemistry an d Biophysics Reports 2 (2015) 115–122. doi:https://doi.org/10.1016/j.bbrep.2015.05.012. 39 URL https://www.sciencedirect.com...

    2015 doi

  5. [13]

    H¨ opfner, U

    M. H¨ opfner, U. Rothe, G. B. and, Biosensor-based evaluation of liposomal b ehav- ior in the target binding process, Journal of Liposome Research 18 (1) (2008) 71–82, pMID: 18348073. arXiv:https://doi.org/10.1080/08982100801894000, doi:10.1080/ 08982100801894000. URL https://...

    2008 doi

  6. [14]

    R. S. Armen, O. D. Uitto, S. E. Feller, Phospholipid component volum es: Determination and application to bilayer structure calculations, Biophysical Journal 75 (1998) 734–744. doi: 10.1016/s0006-3495(98)77563-0

    1998 doi

  7. [15]

    A. P. Dabkowska, D. J. Barlow, A. V. Hughes, R. A. Campbell, P. J. Quinn, M. J. Lawrence, The effect of neutral helper lipids on the structure of cationic lipi d monolayers, J. R. Soc. Interface 9 (2012) 548–561. doi:10.1098/rsif.2011.0356

    2012

  8. [16]

    J. Pan, F. A. Heberle, S. Tristram-Nagle, M. Szymanski, M. Koepfinger , J. Katsaras, N. Kuˇ cerka, Molecular structures of fluid phase phosphatidylglycerol bilayers as determined by small angle neutron and x-ray scattering, Biochimica et Biophysic a Acta (BBA) - Biomem- branes 1...

    2012 doi

  9. [17]

    V. F. Sears, Neutron scattering lengths and cross sections, Neutron New s 3 (1992) 26–37. doi:10.1080/10448639208218770

    1992 doi

  10. [18]

    A. R. J. Nelson, S. W. Prescott, refnx: neutron and X-ray reflectometry analysis in Python, Journal of Applied Crystallography 52 (1) (2019) 193–200. doi:10.1107/ S1600576718017296. URL https://doi.org/10.1107/S1600576718017296

    2019 doi

  11. [19]

    S. Chiu, E. Jakobsson, S. Subramaniam, H. Scott, Combined monte carlo an d molecular dynamics simulation of fully hydrated dioleyl and palmitoyl-oleyl ph osphatidylcholine lipid bilayers, Biophysical Journal 77 (5) (1999) 2462–2469. doi:https://doi.org/10.1016/ S0006-3495(99)7...

    1999

  12. [20]

    Pabst, S

    G. Pabst, S. Danner, S. Karmakar, G. Deutsch, V. A. Raghunathan, On the p ropensity of phosphatidylglycerols to form interdigitated phases, Biophys J 93 (2) ( 2007) 513–525

    2007

  13. [21]

    McKinley, Neutron reflectivity studies of bacterial membranes , peptides and proteins, Ph.D

    L. McKinley, Neutron reflectivity studies of bacterial membranes , peptides and proteins, Ph.D. thesis, Edinburgh University (2017). 40

    2017

  14. [22]

    Perozo, D

    E. Perozo, D. M. Cortes, P. Sompornpisut, A. Kloda, B. Martinac, Open channel structure 41 of mscl and the gating mechanism of mechanosensitive channels, Nature 418 ( 6901) (2002) 942–948

    2002

  15. [23]

    J. S. Najem, M. D. Dunlap, I. D. Rowe, E. C. Freeman, J. W. Grant, S . Sukharev, D. J. Leo, Activation of bacterial channel mscl in mechanically stimulated drople t interface bilayers, Scientific Reports 5 (1) (2015) 13726. URL https://doi.org/10.1038/srep13726

    2015 doi

  16. [24]

    Martinac, P

    B. Martinac, P. R. Rohde, A. R. Battle, E. Petrov, P. Pal, A. F. W. Foo, V. V´ asquez, T. Huynh, A. Kloda, Studying Mechanosensitive Ion Channels Using Liposomes, Human a Press, Totowa, NJ, 2010, pp. 31–53. doi:10.1007/978-1-60761-447-0_4 . URL https://doi.org/10.1007/978-1-60...

    2010 doi

  17. [25]

    Takeda, M

    M. Takeda, M. Kainosho, Cell-free protein production for nmr studi es, Methods in Molecular Biology 831 (2012) 71–84

    2012

  18. [26]

    Hammouda, A new guinier–porod model, Journal of Applied Crystallograph y 43 (4) (2010) 716–719

    B. Hammouda, A new guinier–porod model, Journal of Applied Crystallograph y 43 (4) (2010) 716–719

    2010

  19. [27]

    Irena, nika Manuals 1.5.1, Guinier Porod irena and nika manuals 1.5.1 do cumentation, https: //saxs-igorcodedocs.readthedocs.io/en/stable/Irena/GuinierPorod.html, accessed: 2020-09-14 (2020)

    2020

  20. [28]

    Delhi, Radius of Gyration, http://www.scfbio-iitd.res.in/software/proteomics/rg

    I. Delhi, Radius of Gyration, http://www.scfbio-iitd.res.in/software/proteomics/rg. jsp, accessed: 2020-10-14

    2020

  21. [29]

    Van Der Spoel, E

    D. Van Der Spoel, E. Lindahl, B. Hess, G. Groenhof, A. E. Mark, H. J. Be rendsen, Gromacs: fast, flexible, and free, Journal of computational chemistry 26 (16) (2005) 1701–1718

    2005

  22. [30]

    Chang, R

    G. Chang, R. H. Spencer, A. T. Lee, M. T. Barclay, D. C. Rees, Struct ure of the mscl homolog from mycobacterium tuberculosis: a gated mechanosensitive ion channe l, Science 282 (5397) (1998) 2220–2226

    1998

  23. [31]

    Xie, G.-H

    J.-Y. Xie, G.-H. Ding, Studies on sensitivity to tension and gating p athway of mscl by molec- ular dynamic simulation, Acta Mechanica Sinica 29 (2) (2013) 256–266

    2013

  24. [32]

    P. W. Rose, B. Beran, C. Bi, W. F. Bluhm, D. Dimitropoulos, D. S. Go odsell, A. Prli´ c, M. Quesada, G. B. Quinn, J. D. Westbrook, et al., The rcsb protein dat a bank: redesigned web site and web services, Nucleic acids research 39 (suppl

  25. [34]

    N. Bavi, A. D. Martinac, D. M. Cortes, O. Bavi, P. Ridone, T. Nomura, A. P . Hill, B. Martinac, E. Perozo, Structural dynamics of the mscl c-terminal domain, Scient ific reports 7 (1) (2017) 17229

    2017

  26. [35]

    Martinac, J

    B. Martinac, J. Adler, C. Kung, Mechanosensitive ion channels of e. c oli activated by am- phipaths, Nature 348 (6298) (1990) 261–263

    1990

  27. [36]

    Strutt, J

    R. Strutt, J. W. Hindley, J. Gregg, P. J. Booth, J. D. Harling, R. V. Law , M. S. Friddin, O. Ces, Activating mechanosensitive channels embedded in droplet interface bilayers using membrane asymmetry., Chem Sci 12 (6) (2021) 2138–2145. doi:10.1039/d0sc03889j

    2021 doi

  28. [37]

    S. L. Grage, A. M. Keleshian, T. Turdzeladze, A. R. Battle, W. C. Tay, R. P. May, S. A. Holt, S. A. Contera, M. Haertlein, M. Moulin, et al., Bilayer-mediated clus tering and functional interaction of mscl channels, Biophysical journal 100 (5) (2011) 1252–1260

    2011

  29. [38]

    S. E. Ayscough, M. W. A. Skoda, J. Doutch, A. Caruana, C. Kinane, L. Clifton , S. Titmuss, Tethered Lipid Bilayers as a Platform for Studying the Mechanosensi tive Ion Channel MscL (Mar. 2025). doi:10.5281/zenodo.14975055. URL https://github.com/maxskoda/MscL_tether_NR 42

    2025 doi

  30. [122]

    URL https://www.sciencedirect.com/science/article/pii/ S240558081500031X 55M

    doi:https://doi.org/10.1016/j.bbrep.2015.05.012. URL https://www.sciencedirect.com/science/article/pii/ S240558081500031X 55M. Kowalska, M. Broniatowski, M. Mach, /suppress Lukasz P/suppress lachta, P. Wydro, The effect of the polyethylene glycol chain length of a lipopolymer (...

    2021

Pith tools

Reviewed August 15, 2026 · model on record in the stance chip above.