Incorporation of photoreceptor membrane into a multilamellar film

Rothschild, Kenneth J.; Rosen, K.M.; Clark, Noel A.

doi:10.1016/s0006-3495(80)85039-9

Cited by 26 publications

(20 citation statements)

References 23 publications

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“…The molecular representation of bacteriorhodopsin was generated from the 1.5 Å X-ray structure (28) using the software MOLMOL (29). (31) has been shown to be a rather useful tool to prepare aligned films for NMR experiments (7). It relies on the centrifugation of membrane fragments onto glass disks with simultaneous, or subsequent, partial evaporation of the solvent which aids alignment.…”

Section: Experimental Considerationsmentioning

confidence: 99%

“…A more quantitative approach uses the phospholipid 31 P chemical shift anisotropy (CSA) for assessing the degree of alignment. The CSA tensor is axially symmetric for phospholipids undergoing fast rotation around an axis perpendicular to the bilayer plane.…”

Section: Static 1 H-and 31 P-nmr At the Magic Anglementioning

confidence: 99%

“…4(b). This example shows 31 P spectra of a DMPC sample containing M13 coat protein. The unoriented sample features the powder pattern typical for an axial symmetric CSA tensor, while for the oriented sample all spectral intensity appears at iso .…”

Section: Static 1 H-and 31 P-nmr At the Magic Anglementioning

confidence: 99%

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An introduction to MAS NMR spectroscopy on oriented membrane proteins

Glaubitz

2000

Concepts Magn. Reson.

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Section: Experimental Considerationsmentioning

confidence: 99%

Section: Static 1 H-and 31 P-nmr At the Magic Anglementioning

confidence: 99%

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An introduction to MAS NMR spectroscopy on oriented membrane proteins

Glaubitz

2000

Concepts Magn. Reson.

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“…8,9 The possibility of studying the diffusive behavior of the PRM pigment protein, rhodopsin, was particularly appealing since diffusively mediated intramembrane rhodopsin interactions are considered to play an important role in vision. 10 ' 11 The investigation of membrane protein diffusion more generally by means of PCS-IO offers important advantages since proteins are not labeled and photoabsorption is avoided by a proper choice of laser line.…”

mentioning

confidence: 99%

“…Photoabsorption was avoided because 6471 A is well above the sample absorption band. 9 ting the sample with the evanescent portion of the guided light allowed a well-defined 0.5-Mm-thick region of the sample close to the sample/core interface to be probed 15 by a relatively weak portion (~ 1 mW) of the guided light. Perhaps more importantly for PCS measurements, the incident wave vector of the evanescent light, "£ 0 , was single-valued and well definedo 16 The films used in these studies were formed by depositing bovine retinal rod outer-segment disks onto microscope cover slips using the isopotential ).…”

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confidence: 99%

Study of Multilamellar Films of Photoreceptor Membrane by Photon-Correlation Spectroscopy Combined with Integrated Optics

et al. 1982

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Macroscopic Orientation of Natural and Model Membranes for Structural Studies

Gröbner

Taylor

Williamson

et al. 1997

Analytical Biochemistry

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O ne a p p ro a ch for o b ta in in g h ig h -r eso lu tio n s tr u c tu ra l an d fu n ctio n a l in fo rm a tio n for b iom em b ran es an d th e ir p ro tein s is b y s ta tic so lid -sta te NMR o f o ri e n te d sy stem s. H ere, a g e n e r a l p ro ced u re to a lig n fu lly fu n c tio n a l b io lo g ica l m em b ra n es co n ta in in g large m em b ran e p ro tein s (Mr >30,000) is d escrib ed . T he m eth od , b a sed on th e iso p o te n tia l sp in -d ry u ltra ce n tr ifu g a tio n tech n iq u e , r e lie s on th e cen trifu g a tio n o f m em b ran e fra g m en ts on to a su p p o rt w ith sim u lta n e ous, or su b seq u en t, p a r tia l e v a p o r a tio n o f th e so lv e n t w h ic h a id s a lig n m en t. atu ral m em b ra n es w ith th e red c e ll a n io n ex ch a n g e tran sp ort p r o te in in ery th ro cy tes, b an d 3, an d th e n ico tin ic a c e ty lc h o lin e receptor. O 1997 Academic Press The elucidation of the structural and functional orga nization of biological membranes by various biophysi cal techniques is one of the important questions being addressed in structural biology. The complexity of the systems, however, their supramolecular structure, and their dynamic properties make direct studies particu larly difficult. Specifically, membrane proteins present extraordinary technical difficulties to the most com monly used methods in structural biology, such as crys tallography (1) and solution NMR spectroscopy (2). In 1 To whom correspondence should be addressed, Fax; 01865/275-234 or -259. E-mail: awatts@bioch.ox.ac.uk. 132recent years solid-state NMR spectroscopy (3, 4) on macroscopically oriented lipid bilayers has rapidly emerged as an alternative approach to elucidate struc tural and functional features of membrane-bound pep tides and proteins. In such aligned systems, lipids and proteins are arranged uniaxially around the mem brane, allowing normal orientation of the molecule backbone relative to the substratum. In combination with isotopic labeling (e.g., 2H, 13C, 15N) this NMR ap proach has successfully been used to determine the complete secondary structure of the M2 channel pep tide and fd coat protein (3), while the orientation of the antibiotic peptide magainin has been resolved in bilayers (5). The complete secondary structure of gram icidin and its dynamic properties in membranes have also been obtained using 2H and 15N NMR (6-9). In addition, the complete structure and orientation of deu terated retinal in bacteriorhodopsin at different states of its photocycle has been resolved (10), The average molecular and orientational order of lipids and peptides in liquid crystalline membranes could also be deter mined unambiguously in this way (11-14).Unfortunately, the generation of structural and ori entational information about membrane proteins has been limited mainly to peptides, since no general methods have been available for aligning native and reconstituted membranes containing larger integral membrane proteins in sufficient quality and quantity without affect...

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Incorporation of photoreceptor membrane into a multilamellar film

Cited by 26 publications

References 23 publications

An introduction to MAS NMR spectroscopy on oriented membrane proteins

An introduction to MAS NMR spectroscopy on oriented membrane proteins

Study of Multilamellar Films of Photoreceptor Membrane by Photon-Correlation Spectroscopy Combined with Integrated Optics

Macroscopic Orientation of Natural and Model Membranes for Structural Studies

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