Maikel Rheinstadter

Prof. Maikel Rheinstadter

Department of Physics & Astronomy, McMaster University, Hamilton, ON L8S 4M1, Canada
orcid

Research Focus & Metrics

Academic Career Length

27Years (2000-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 April 2005 in Europhysics Letters
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Journal Article
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MEM. Enderle
M. Enderle
CMC. Mukherjee
C. Mukherjee
BFB. Fåk
B. Fåk
RKR. K. Kremer
R. K. Kremer
JBJ.-M. Broto
J.-M. Broto
HRH. M. Rønnow
H. M. Rønnow

1 June 2010 in Chemistry and Physics of Lipids
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Journal Article
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Georg PabstGeorg Pabst
Georg Pabst
NKNorbert Kučerka
Norbert Kučerka
Mu-Ping NiehMu-Ping Nieh
Mu-Ping Nieh
Maikel RheinstadterMaikel Rheinstadter
Maikel Rheinstadter
JKJohn Katsaras
John Katsaras

14 October 2014 in PeerJ
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Journal Article
Open access
FYFei-Chi Yang
Fei-Chi Yang
YZYuchen Zhang
Yuchen Zhang
Maikel RheinstadterMaikel Rheinstadter
Maikel Rheinstadter
Hair is a filamentous biomaterial consisting mainly of proteins in particular keratin. The structure of human hair is well known: the medulla is a loosely packed, disordered region near the centre of the hair surrounded by the cortex, which contains the major part of the fibre mass, mainly consisting of keratin proteins and structural lipids. The cortex is surrounded by the cuticle, a layer of dead, overlapping cells forming a protective layer around the hair. The corresponding structures have been studied extensively using a variety of different techniques, such as light, electron and atomic force microscopes, and also X-ray diffraction. We were interested in the question how much the molecular hair structure differs from person to person, between male and female hair, hair of different appearances such as colour and waviness. We included hair from parent and child, identical and fraternal twins in the study to see if genetically similar hair would show similar structural features. The molecular structure of the hair samples was studied using high-resolution X-ray diffraction, which covers length scales from molecules up to the organization of secondary structures. Signals due to the coiled-coil phase of α-helical keratin proteins, intermediate keratin filaments in the cortex and from the lipid layers in the cell membrane complex were observed in the specimen of all individuals, with very small deviations. Despite the relatively small number of individuals (12) included in this study, some conclusions can be drawn. While the general features were observed in all individuals and the corresponding molecular structures were almost identical, additional signals were observed in some specimen and assigned to different types of lipids in the cell membrane complex. Genetics seem to play a role in this composition as identical patterns were observed in hair from father and daughter and identical twins, however, not for fraternal twins. Identification and characterization of these features is an important step towards the detection of abnormalities in the molecular structure of hair as a potential diagnostic tool for certain diseases.

3 September 2004 in Physical Review Letters
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Maikel RheinstadterMaikel Rheinstadter
Maikel Rheinstadter
COC. Ollinger
C. Ollinger
GFG. Fragneto
G. Fragneto
Franz DemmelFranz Demmel
Franz Demmel
TST. Salditt
T. Salditt
We have studied the collective short wavelength dynamics in deuterated 1,2-dimyristoyl-sn-glycero-3-phoshatidylcholine (DMPC) bilayers by inelastic neutron scattering. The corresponding dispersion relation ℏω(Q) is presented for the gel and the fluid phase of this model system. The temperature dependence of the inelastic excitations indicates a phase coexistence between the two phases over a broad range and leads to a different assignment of excitations from that reported in a preceding inelastic x-ray scattering study [Phys. Rev. Lett. 86, 740 (2001)]. As a consequence, we find that the minimum in the dispersion relation is actually deeper in the gel than in the fluid phase. Finally, we can clearly identify an additional nondispersive (optical) mode predicted by molecular dynamics simulations [Phys. Rev. Lett. 87, 238101 (2001)]. DOI: http://dx.doi.org/10.1103/PhysRevLett.93.108107 © 2004 The American Physical Society

18 June 2013 in PLOS ONE
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CAClare L. Armstrong
Clare L. Armstrong
DMDrew Marquardt
Drew Marquardt
HDHannah Dies
Hannah Dies
NKNorbert Kučerka
Norbert Kučerka
ZYZahra Yamani
Zahra Yamani
Maikel RheinstadterMaikel Rheinstadter
Maikel Rheinstadter
Rafts, or functional domains, are transient nano- or mesoscopic structures in the exoplasmic leaflet of the plasma membrane, and are thought to be essential for many cellular processes. Using neutron diffraction and computer modelling, we present evidence for the existence of highly ordered lipid domains in the cholesterol-rich (32.5 mol%) liquid-ordered ( ) phase of dipalmitoylphosphatidylcholine membranes. The liquid ordered phase in one-component lipid membranes has previously been thought to be a homogeneous phase. The presence of highly ordered lipid domains embedded in a disordered lipid matrix implies non-uniform distribution of cholesterol between the two phases. The experimental results are in excellent agreement with recent computer simulations of DPPC/cholesterol complexes [Meinhardt, Vink and Schmid (2013). Proc Natl Acad Sci USA 110(12): 4476–4481], which reported the existence of nanometer size domains in a liquid disordered lipid environment.

14 January 2009 in Physical Review E
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EFElijah Flenner
Elijah Flenner
JDJhuma Das
Jhuma Das
Maikel RheinstadterMaikel Rheinstadter
Maikel Rheinstadter
IKIoan Kosztin
Ioan Kosztin
We use a long, all-atom molecular-dynamics (MD) simulation combined with theoretical modeling to investigate the dynamics of selected lipid atoms and lipid molecules in a hydrated diyristoyl-phosphatidylcholine lipid bilayer. From the analysis of a 0.1μs MD trajectory, we find that the time evolution of the mean-square displacement, ⟨[δr(t)]2⟩, of lipid atoms and molecules exhibits three well-separated dynamical regions: (i) ballistic, with ⟨[δr(t)]2⟩∼t2 for t≲10fs; (ii) subdiffusive, with ⟨[δr(t)]2⟩∼tβ with β<1 for 10ps≲t≲10ns; and (iii) Fickian diffusion, with ⟨[δr(t)]2⟩∼t for t≳30ns. We propose a memory-function approach for calculating ⟨[δr(t)]2⟩ over the entire time range extending from the ballistic to the Fickian diffusion regimes. The results are in very good agreement with the ones from the MD simulations. We also examine the implications of the presence of the subdiffusive dynamics of lipids on the self-intermediate scattering function and the incoherent dynamic structure factor measured in neutron-scattering experiments.