Linear dichroism and the orientation of reaction centers of Rhodopseudomonas sphaeroides in dried gelatin films.

Aqueous mixtures of reaction centers of Rhodopseudomonas sphaeroides and gelatin were dried to form thin films. Following hydration, these films were stretched as much as two to three times their original length. Polarized absorption spectra showing linear dichroism were obtained for both unstretched and stretched films, with the planes and stretching axes of the films mounted in various geometries relative to the electric vector of the measuring beam. These data were analyzed in terms of the following model: Reaction centers possess an axis of symmetry that is fixed in relation to the reaction center structure. In unstretched films this axis is confined to the film plane and oriented at random within the plane. In stretched films the symmetry axis is aligned with the direction of stretching. In both preparations reaction centers are distributed randomly with respect to rotation about the axis of symmetry. The data are consistent with this model when the analysis acknowledges less than perfect orientation. For perfect orientation in a stretched film the model predicts uniaxial symmetry about the axis of stretching. The approach to this condition was examined with films stretched to different extents. Extrapolation yielded dichroic ratios for the ideal case of perfect orientation, and allowed calculation of the angles between the axis of symmetry and the various optical transition dipoles in the reaction center. This treatment included the two absorption bands of the bacteriochlorophyll 'special pair' (photochemical electron donor) in the Qx region, at 600 and 630 nm, which we were able to resolve in light minus dark difference spectra.     

Linear dichroism and the orientation of reaction centers of Rhodopseudomonas sphaeroides in dried gelatin films

Aqueous mixtures of reaction centers of Rhodopseudomonas sphaeroides and gelatin were dried to form thin films. Following hydration, these films were stretched as much as two to three times their original length. Polarized absorption spectra showing linear dichroism were obtained for both unstretched and stretched films, with the planes and stretching axes of the films mounted in various geometries relative to the electric vector of the measuring beam. These data were analyzed in terms of the following model: Reaction centers possess an axis of symmetry that is fixed in relation to the reaction center structure. In unstretched films this axis is confined to the film plane and oriented at random within the plane. In stretched films the symmetry axis is aligned with the direction of stretching. In both preparations reaction centers are distributed randomly with respect to rotation about the axis of symmetry. The data are consistent with this model when the analysis acknowledges less than perfect orientation. For perfect orientation in a stretched film the model predicts uniaxial symmetry about the axis of stretching. The approach to this condition was examined with films stretched to different extents. Extrapolation yielded dichroic ratios for the ideal case of perfect orientation, and allowed calculation of the angles between the axis of symmetry and the various optical transition dipoles in the reaction center. This treatment included the two absorption bands of the bacteriochlorophyll ‘special pair’ (photochemical electron donor) in the Q_x region, at 600 and 630 nm, which we were able to resolve in light minus dark difference spectra.     

Infrared dichroism of polynucleotides of repeated sequence. I. Poly(dA)·poly(dT) and poly[d(A-T)]·poly[d(A-T)]

Infrared dichroism measurements of oriented films of poly(dA)·poly(dT) and poly[d(A-T)]·poly[d(A-T)] have been made under the conditions of low salts content and high humidity for which the geometry is known. The angles which the transition moments make with the helix axis are compared with the orientations of the corresponding bonds. Except for the in-plane base model of poly[(A-T)]·poly[d(A-T)], there is no agreement. This may imply either that a model which assumes bonds and transition moments to be colinear is not acceptable or that x-ray data are inaccurate. These possibilities are discussed especially with respect to phosphate group orientation. An appendix gives the derivations of dichroic-ratio expressions for helical molecules of different symmetry types.     

The orientations of reaction center transition moments in the chromatophore membrane of Rhodopseudomonas sphareroides, bases on new linear dichroism and photoselection measurements.

Chromatophore membranes from Rhodopseudomonas sphaeroides were oriented by drying suspensions on the surfaces of glass slides, Polarized spectra of light-induced absorption changes were obtained between 500 and 1000 nm. As observed earlier, these spectra showed negative bands, reflecting photooxidation of the bacteriochlorophyll 'special pair' in the reaction centers, centered near 870, 810, 630 and 600 nm. These bands have been designated BY1, BY2, BX1 and BX2, respectively, corresponding to two QY transitions and two QX transitions of the dimeric special pair. We found the BY1 and BX1 transition moments to be parallel (within 20 degrees) to the plane of the membrane, whereas the BX2 moment makes an angle of 55--63 degrees with the plane. Using the photoselection technique we found that the angle between the BY1 and BX1 transition moments is 30 degrees, while that between BY1 and BX2 is 75 degrees. The BX1 and BX2 moments were found to be orthogonal, consistent with the prediction of molecular exciton theory for a dimer. By combining these data, we have calculated the orientations of the transition moments of the bacteriochlorophyll dimer in spherical polar coordinates, with the pole of the coordinate system normal to the plane of the membrane. The orientations of the QY and QX transition moments of the two bacteriopheophytin molecules in the reaction center were also computed in this coordinate system by transforming the data reported by Clayton, C.N., Rafferty, R.K. and Vermeglio, A. ((1979) Biochim. Biophys. Acta 545, 58--68). We have derived the transformation equations for two polar coordinate systems: in one, the pole is an axis of symmetry as defined by the orientations of purified reaction centers in stretched gelatin films (Rafferty, C.N. and Clayton, R.K. (1979) Biochim. Biophys. Acta 545, 106--121). In the other, the pole is normal to the plane of the chromatophore membrane. These two polar axes are approximately orthogonal.     

Quantum-mechanical theory of CD for infinite helical polymers

Quantum-mechanical equations are derived that are particularly well suited to actual computations of the CD for helical polymers. They make use of cyclic boundary conditions and helical symmetry, so that only two matrices with a size equal to the number of transitions considered need be diagonalized. The final equations are expressed directly in terms of monomer properties and helical parameters to invite the same input as earlier calculations, and are given as a rotational strength times a shape function for ease of comparison with the earlier work. The shape of the helix term is expressed as a derivative with respect to ω and depends on the distance between monomers along the helix axis. Other terms involving two electric transition dipoles depend on the distance from the helix axis to the transition center. These equations are directly comparable to the classical equations derived for cyclic boundary conditions and helical symmetry. We present an outline of the derivation and enough intermediate steps to clarify how the equations arise.     

Fluorescence polarization in a planar array of pigment molecules: theoretical treatment and application to flavins incorporated into artificial membranes.

A quantitative fluorescence polarization theory of molecules bound to two-dimensional plane layers has been developed when the electronic transition moments of absorption and emission are parallel within the fluorescent molecules. The transition moments are assumed to be in preferred orientation with respect to the normal to the plane and to be randomly oriented within the plane (rotational symmetry with the normal as axis of symmetry). Three basic model distributions of transition moments are investigated quantitatively. These model distributions represent a simplification but in most cases may be expected to describe reality with sufficient accuracy. For all distributions, two cases of different mobility of molecules are treated: (a) the lifetime of fluorescence is small compared with the characteristic relaxation time of the distribution, and (b) the lifetime of fluorescence is long, so that a complete reorientation of transition moments during the excited state can take place. From the quantitative calculations four characteristic quantities are derived, which are appropriate for the analysis of experimental data. Experiments are carried out with phosphatidylcholine bilayer membranes which contain three differently substituted amphiphilic flavins. All three flavins yield similar data. Their analyses predict free and fast mobility of the flavin chromophore.     

Asymmetry in structure of in termediate and large neurons of frog retinal ganglion layer

We have carried out a morphometric investigation of the symmetry of intermediate (type II) and large (types III and V) ganglion cells on silver-impregnated retinal wholemounts of frog retina. We selected the nucleolus of theneuron and the axis passing through the nucleolus in the direction of the optic disk (central and bilateral symmetry) as elements of symmetry. We have shown that the dendritic ramification angles of all cell types are smaller than 360° and those of type II cells smaller than 180°; the cell somata do not lie in the center of the dendritic field and consequently the ganglion cells do not possess radial symmetry. In the vast majority of ganglion cells the directions of the start of the axon and dendrites are opposite to each other, the dendrites being oriented in the direction from the retinal center towards the periphery in all quadrants of the retinal map. For the estimation of the bilateral symmetry we measured the distance from the most remote dendritic terminals to the axis on the left and right of the axis, and counted the number of ramification knots and basal dendrites. We established that the majority of ganglion cells are asymmetrical as regards two or three of the characteristics mentioned. Consequently the asymmetrical structure of ganglion cells of the frog is a normal characteristic rather than an exception. The correlation between the asymmetry of the structure of ganglion cells and the functional asymmetry of their receptive fields is discussed.N. I. Lobachevskii Research Institute of Applied Mathematics and Cybernetics, University of Gorki. Translated from Neirofiziologiya, Vol. 17, No. 4, pp. 456–462, July–August, 1985.     

The orientations of reaction center transition moments in the chromatophore membrane of Rhodopseudomonas sphaeroides, based on new linear dichroism and photoselection measurements

Chromatophore membranes from Rhodopseudomonas sphaeroides were oriented by drying suspensions on the surfaces of glass slides. Polarized spectra of light-induced absorption changes were obtained between 500 and 1000 nm. As observed earlier, these spectra showed negative bands, reflecting photooxidation of the bacteriochlorophyll ‘special pair’ in the reaction centers, centered near 870, 810, 630 and 600 nm. These bands have been designated BY₁, BY₂, BX₁ and BX₂, respectively, corresponding to two Q_y transitions and two Q_x transitions of the dimeric special pair. We found the BY₁ and BX₁ transition moments to be parallel (within 20°) to the plane of the membrane, whereas the BX₂ moment makes an angle of 55–63° with the plane.Using the photoselection technique we found that the angle between the BY₁ and BX₁ transition moments is 30°, while that between BY₁ and BX₂ is 75°. The BX₁ and BX₂ moments were found to be orthogonal, consistent with the prediction of molecular exciton theory for a dimer.By combining these data, we have calculated the orientations of the transition moments of the bacteriochlorophyll dimer in spherical polar coordinates, with the pole of the coordinate system normal to the plane of the membrane. The orientations of the Q_y and Q_x transition moments of the two bacteriopheophytin molecules in the reaction center were also computed in this coordinate system by transforming the data reported by Clayton, C.N., Rafferty, R.K. and Vermeglio, A. ((1979) Biochim. Biophys. Acta 545, 58–68). We have derived the transformation equations for two polar coordinate systems: in one, the pole is an axis of symmetry as defined by the orientations of purified reaction centers in stretched gelatin films (Rafferty, C.N. and Clayton, R.K. (1979) Biochim. Biophys. Acta 545, 106–121). In the other, the pole is normal to the plane of the chromatophore membrane. These two polar axes are approximately orthogonal.     

Orientation of reaction center and antenna chromophores in the photosynthetic membrane of rhodopseudomonas viridis

Whole cells of Rhodopseudomonas viridis were oriented in a magnetic field. The degree of orientation of the cells was determined by using a photoselection technique. In order to deduce the orientation of the antennae and chromophores of the reaction centers with respect to the membrane plane, we performed linear dichroism measurements of absolute spectra and light induced difference spectra linked to states P⁺I and PI^? on oriented cells. These measurements lead to the following conclusions:The antennae bacteriochlorophyll molecular plane is nearly perpendicular to the membrane. The Q_y and Q_x transitions moments of these molecules make respectively angles of 20 and 70°ith the membrane plane. The antenna carotenoid molecules make an angle of 45°ith the membrane.The primary electron donor possesses two transition moments centered respectively at 970 and 850 nm. The 970 nm transition moment is parallel to the membrane plane, the 850 nm transition is tilted out of the plane. Upon photooxidation of this primary electron donor, a monomer-like absorption band appears at 805 nm. Its transition makes an angle smaller than 25° with the membrane. The photooxidation of the dimer also induces an absorption band shift for the two other bacteriochlorophyll molecules of the reaction center. The absorption band shifts of the two bacteriochlorophyll molecules occur in opposite direction.One bacteriopheophytin molecule is photoreduced in state PI^?. This photoreduction induces an absorption band shift for only one bacteriochlorophyll molecule. Finally, the geometry of the dimeric primary donor seems to be affected by the presence of a negative charge in the reaction center.     

Polarised absorption spectroscopy of chlorophyll-lipid membranes

A technique has been developed for measuring visible absorption spectra of chlorophyll in lipid membranes. An expression is derived which enables the directions of the transition moments of the different absorption bands to be determined from polarisation data. It is found that the transition moments of the principal blue and red absorption bands of chlorophyll a make angles of 26° and 36.5° respectively with the plane of the membrane. On the assumption that these two transitions lie in the plane of the porphyrin ring and are mutually perpendicular, it may be deduced that the plane of the porphyrin ring is tilted at approx. 48° to the membrane surface. For chlorophyll b the transition moments of the blue and red bands are found to make angles of 29.5° and 36.5° with the plane of the bilayer, giving an angle of tilt of the porphyrin ring of approx. 51°.

These results are compared with measurements of dichroism in vivo.     

Polarized vibrational spectroscopy of fiber polymers: hydrogen bonding in cellulose II

Vibrational spectroscopy using polarized incident radiation can be used to determine the orientation of X-H bonds with respect to coordinates such as crystallographic axes. The adaptation of this approach to polymer fibers is described here. It requires spectral intensity to be quantified around a 180 degrees range of polarization angles and not just recorded transversely and longitudinally as is normal in fiber spectroscopy. Mercerized cellulose II is used as an example. The unit cell of the cellulose II lattice contains six distinct hydroxyl groups engaged in a complex network of hydrogen bonds that hold the cellulose chains laterally together. A formalism is described to relate the variation in intensity of each O-H stretching mode to the angle between its transition moment and the chain axis as the polarization axis is rotated with respect to the fiber axis. It was necessary to include the effect of dispersion in chain orientation around the mean and the averaging of all rotational positions of the chains round their axis. The two crystallographically distinct O(2)-H groups, which are each hydrogen-bonded to only one acceptor oxygen, show a close match in orientation between the transition moments of their stretching bands and the O-H bond axis. The two O(3)-H groups each have a three-centered hydrogen bond to O-5 and O-6 of the next residue in the same chain. The transition moments of their stretching modes lay between the acceptor oxygens. Hydrogen bonding from the O(6)-H groups is still more complex but again the transition moment of each O-H bond lay within the cone of orientations described by the acceptor oxygens, provided that one additional acceptor oxygen excluded from the published crystal structure was considered. The transition moments for the O-H stretching modes were approximately aligned with the O-H bond axes, but the alignment was not necessarily exact. This approach is not restricted to hydroxyl groups, but it is particularly useful for the elucidation of hydrogen bonding in fibrous polymers for which crystallographic data on proton positions are not available.     

Nonaxiality in infrared dichroic ratios of polytopic transmembrane proteins.

In polytopic alpha-helical transmembrane proteins, the distribution of amide vibrational transition moments can be nonaxial, if the helix axes are tilted relative to the symmetry axis of the helix bundle. The infrared dichroic ratios from oriented samples then contain nonaxial terms and, in the most general case, require a second-order parameter for the axis of the helix bundle. The extent of nonaxiality depends on the summation over the individual amide transition moments along the helix. Because this is strongly oscillatory, with a 3.6-residue periodicity, complete axial symmetry is not achieved rapidly on progressive summation. Expressions for the contributions of residual nonaxiality to the dichroic ratios are derived. A similar situation arises for oligomers of transmembrane beta-barrel proteins, e.g., the porin trimer. In this case, the extent of nonaxiality depends not only on the number of residues in the beta-barrel, but also on the tilt of the beta-strands relative to the barrel axis and the characteristic dimensions of a beta-sheet, which together determine the axial periodicity. The nonaxial contributions to the dichroic ratios of beta-barrel oligomers are also derived. Estimates are given of the likely size of the nonaxial contributions for the different alpha-helical and beta-sheet systems.     

Polarized fluorescence measurements on ordered photosynthetic antenna complexes: Chlorosomes of Chloroflexus aurantiacus and B800-B850 antenna complexes of Rhodobacter sphaeroides

We have used a new and relatively easy approach to study the pigment-organization in chlorosomes from the photosynthetic bacterium Chloroflexus aurantiacus and in B800-850 antenna complexes of the photosynthetic purple bacterium Rhodobacter sphaeroides. These particles were embedded in compressed and uncompressed gels and the polarized fluorescence was determined in a 90° setup. Assuming both a rotational symmetric distribution of the particles in the gel and of the transition dipole moments in the particles, the order parameters <P₂> and <P₄>, describing the orientation of the symmetry axis of the particles with respect to the direction of gel expansion can be determined. Moreover, the direction parameters, describing the orientation of the absorption and emission dipole moments with respect to the symmetry axis of the particles can be obtained.

The value of <P₂> is essential for quantitative interpretation of linear dichroism measurements and usually it is estimated from theoretical approaches, which may lead to incorrect results. For the rod-like chlorosomes the value of <P₂> appears to be the same as predicted by the theoretical approach of Ganago, A. O., M. V. Fok, I. A. Abdourakhmanov, A. A. Solov'ev, and Yu. E. Erokhin (1980. Mol. Biol. [Mosc.]. 14:381-389). The agreement with linear dichroism results, analyzed with this theoretical approach shows that the transition dipole moments are indeed in good approximation distributed in a rotationally symmetric way around the long axis of the chlorosomes. Moreover, it appears those BChl c molecules, which fluoresce, are oriented in the same way with respect to the symmetry axis as the rest of these pigments, with the dipole moments close to parallel to the long axis.

The B800-850 complexes appear to orient like discs, whereas the transition dipoles of the BChl a 800- and 850-nm bands are oriented almost perpendicular to the symmetry axis. These findings are in agreement with the minimal model for these complexes proposed by Kramer, H. J. M., R. van Grondelle, C. N. Hunter, W. H. J. Westerhuis, and J. Amesz (1984. Biochim. Biophys. Acta. 156-165).

The amount of orientation of the particles appears to vary for different gels and it is lower than predicted by the theory of Ganago et al., showing that application of their approach for these particles leads to incorrect interpretations.

The approach that is used in this study allows determination of orientations of those dipole moments, which transfer their excitation energy to the fluorescing species, in contrast to linear dichroism measurements, where the orientations of all absorbing dipole moments are studied. For the polarized fluorescence measurements, the amount of orientation of the particles is determined experimentally, whereas for linear dichroism this amount has to be estimated from theoretical models. The value of <P₂> that can be determined from the fluorescence measurements can, however, also be used for a quantitative interpretation of the linear dichroism results.

     

Study of the reorientation of coenzyme in active sites of aspartate-aminotransferase isoenzymes using linear dichroism method

Cytosolic and mitochondrial pig aspartate aminotransferases (cAAT and mAAT) and chicken cAAT were oriented in a compressed slab of polyacrylamide gel. Linear dichroism (LD) spectra of the pyridoxal and pyridoxamine forms of AATs and of complexes of the pyridoxal form with substrate analogues have been recorded. The tilt angles of the coenzyme at the intermediary steps of the transamination reaction have been calculated on the basis of reduced LD values (delta A/A), atomic coordinates of the coenzyme and directions of the transition dipole moments in the coenzyme ring. It was assumed that rotation of the coenzyme ring occurs around the C2-C5 axis in all cases except the enzyme complex with glutarate: in the latter case the direction N1-C4 was assumed to be a rotation axis. It has been found that formation of the enzyme complex with glutarate and protonation of the internal aldimine induce dissimilar reorientations of the coenzyme. As a result of protonation, the coenzyme tilts by 27 degrees in cAAT and 13 degrees in mAAT. Formation of the external aldimine with 2-methylaspartate is accompanied by tilting of the coenzyme ring by 44 degrees in cAAT and 39 degrees in mAAT. For the quinonoid complex with erythro-3-hydroxyaspartate, the tilt angles were found to be 63 degrees in cAAT and 53 degrees in mAAT. It was inferred that the basic features of the active site dynamics are similar in three AATs studied. The differences in the coenzyme tilt angles between cAAT and mAAT might be linked to catalytic peculiarities of the isoenzymes.     

Absorption and fluorescence spectra and molecular organization of bacteriochlorophyll in reaction centers of Rhodopseudomonas spheroides

Second derivative spectroscopy, computer curve analysis and Stepanov's equation show that the absorbance and fluorescence spectra of primary electron donor in reaction center of Rhodopseudomonas sphaeroides are splitting each into two asymmetric Gaussian components. Their absorption maxima at -196 degrees are 880 and 896 nm and emission maxima-906 and 923 nm, respectively. The absorption spectrum of Bchl-800 splits in the near infrared region into two bands with maxima at 790 and 803 nm. These components are ascribed to an exciton coupling in the two dimers of bacteriochlorophyll in the reaction center. The Qy transition moments of the two bacteriochlorophyll molecules of primary electron donor make an angle of 110 degrees and the angle between two Qy transitions of the pigment in Bchl-800 dimer is 150 degrees. The distance between the centers of chromophores in the dimers is estimated to be 8-11 A.     

Conformational analysis of phosphatidylethanol-amine in multilayers by infrared dichroism.

Built-up films of L-alpha-dipalmitoyl phosphatidylethanolamine were prepared. Infrared dichroism was measured for the sample and analysed by a new method. This method has been developed for the determination of the directions of transition moments in a film sample, in which there is an axis of symmetry of perpendicular to the film plane. The directions of transition moments were determined for the six vibrations assigned to the CH2 antisymmetric stretching, CH2 symmetric stretching, CH2 scissoring, C=O stretching, PO2- antisymmetric stretching, and C-C-N+ antisymmetric stretching modes. The results indicate that hydrocarbon chains are inclined at about 75 degrees to the film plane and the polar groups orient parallel to the plane in the builtup film. A structural model of the phosphatidylethanolamine in the built-up film is proposed.     

Physico-chemical study of the complexes of "33258 Hoechst" with DNA and nucleohistone.

The degree of binding of "33258 Hoechst" to DNA and nucleohistone has been determined by equilibrium dialysis and the properties of the complexes have been followed by different optical and electro-optical methods, after determining the orientation of the main transition moments within the dye molecule. The binding isotherm was found composed of a Langmuir-type and of a strongly cooperative component. The existence of two bound species yielded a continuous variation of most of the properties of the complexes studied as the amount of binding increased, while the hydrodynamic properties of the macromolecules were not affected. At low binding, the strongly bound dye molecules appeared to bind to highly fluorescent sites with their long axis oriented at 45 degree to the helix axis. As the binding proceeds, less fluorescent sites are cooperatively occupied and the inclination of these ligand molecules becomes closer to that of the base planes. These results are compatible with the formation of two external complexes with the double helical structure.     

Symmetry of septin hourglass and ring structures

Septin filaments form ordered hourglass and ring-shaped structures in close apposition to the yeast bud-neck membrane. The septin hourglass scaffolds the asymmetric localization of many essential cell division proteins. However, it is unknown whether the septin structures have an overall polarity along the mother-daughter axis that determines the asymmetric protein localization. Here we engineered rigid septin- green fluorescent protein (GFP) fusions with various fluorescence dipole directions by changing the position of the GFP beta-barrel relative to the septin filament axis. We then used polarized fluorescence microscopy to detect potential asymmetries in the filament organization. We found that both the hourglass and ring filament assemblies have sub-resolution C(2) symmetry and lack net polarity along the mother-daughter axis. The hourglass filaments have an additional degree of symmetry relative to the ring filaments, most likely due to a twist in their higher-order structure. We previously reported that during the hourglass to rings transition septin filaments change their direction. Here we show that the filaments also undergo a change in their lateral organization, consistent with filament untwisting. The lack of net septin polarity along the mother-daughter axis suggests that there are no septin-based structural reasons for the observed asymmetry of other proteins. We discuss possible anisotropic processes that could break the septin symmetry and establish the essential bud-neck asymmetry.     

Experimental verification of a computational technique for determining ground reactions in human bipedal stance

We have developed a three-dimensional (3D) biomechanical model of human standing that enables us to study the mechanisms of posture and balance simultaneously in various directions in space. Since the two feet are on the ground, the system defines a kinematically closed-chain which has redundancy problems that cannot be resolved using the laws of mechanics alone. We have developed a computational (optimization) technique that avoids the problems with the closed-chain formulation thus giving users of such models the ability to make predictions of joint moments, and potentially, muscle activations using more sophisticated musculoskeletal models. This paper describes the experimental verification of the computational technique that is used to estimate the ground reaction vector acting on an unconstrained foot while the other foot is attached to the ground, thus allowing human bipedal standing to be analyzed as an open-chain system. The computational approach was verified in terms of its ability to predict lower extremity joint moments derived from inverse dynamic simulations performed on data acquired from four able-bodied volunteers standing in various postures on force platforms. Sensitivity analyses performed with model simulations indicated which ground reaction force (GRF) and center of pressure (COP) components were most critical for providing better estimates of the joint moments. Overall, the joint moments predicted by the optimization approach are strongly correlated with the joint moments computed using the experimentally measured GRF and COP (0.78 < or = r(2) < or = 0.99,median,0.96) with a best-fit that was not statistically different from a straight line with unity slope (experimental=computational results) for postures of the four subjects examined. These results indicate that this model-based technique can be relied upon to predict reasonable and consistent estimates of the joint moments using the predicted GRF and COP for most standing postures.     

Electronic transitions in the isoalloxazine ring and orientation of flavins in model membranes studied by polarized light spectroscopy.

The orientation of flavin mononucleotide (FMN) in model membranes and the directions of the transition moments of the first three bands in the electronic absorption spectrum of the oxidized form of the isoalloxazine ring have been determined by means of linear dichroism and polarized fluorescence spectroscopy. Measured counterclockwise relative to the axis connecting the two nitrogens in the central ring (considered positive when going in the direction from -CN less than to greater than or equal to N), these angles are 58 +/- 4 degrees (450-nm band), 97 +/- 3 degrees (350-nm band), and 119 +/- 2 degrees (260-nm band).