Vectorially oriented monolayers of the cytochrome c/cytochrome oxidase bimolecular complex.

Vectorially oriented monolayers of yeast cytochrome c and its bimolecular complex with bovine heart cytochrome c oxidase have been formed by self-assembly from solution. Both quartz and Ge/Si multilayer substrates were chemical vapor deposited with an amine-terminated alkylsiloxane monolayer that was then reacted with a hetero-bifunctional cross-linking reagent, and the resulting maleimide endgroup surface then provided for covalent interactions with the naturally occurring single surface cysteine 102 of the yeast cytochrome c. The bimolecular complex was formed by further incubating these cytochrome c monolayers in detergent-solubilized cytochrome oxidase. The sequential formation of such monolayers and the vectorially oriented nature of the cytochrome oxidase was studied via meridional x-ray diffraction, which directly provided electron density profiles of the protein(s) along the axis normal to the substrate plane. The nature of these profiles is consistent with previous work performed on vectorially oriented monolayers of either cytochrome c or cytochrome oxidase alone. Furthermore, optical spectroscopy has indicated that the rate of binding of cytochrome oxidase to the cytochrome c monolayer is an order of magnitude faster than the binding of cytochrome oxidase to an amine-terminated surface that was meant to mimic the ring of lysine residues around the heme edge of cytochrome c, which are known to be involved in the binding of this protein to cytochrome oxidase.

Vectorially oriented monolayers of detergent-solubilized Ca(2+) -ATPase from sarcoplasmic reticulum.

A method for tethering proteins to solid surfaces has been utilized to form vectorially oriented monolayers of the detergent-solubilized integral membrane protein Ca(2+) -ATPase from the sarcoplasmic reticulum (SR). Bifunctional, organic self-assembled monolayers (SAMs) possessing "headgroup" binding specificity for the substrate and "endgroup" binding specificity for the enzyme were utilized to tether the enzyme to the substrate. Specifically, an amine-terminated 11-siloxyundecaneamine SAM was found to bind the Ca(2+)-ATPase primarily electrostatically. The Ca(2+)-ATPase was labeled with the fluorescent probe 5-(2-[(iodoacetyl)amino]ethyl)aminonaphthalene-1-sulfonic acid before monolayer formation. Consequently, fluorescence measurements performed on amine-terminated SAM/enzyme monolayers formed on quartz substrates served to establish the nature of protein binding. Formation of the monolayers on inorganic multilayer substrates fabricated by molecular beam epitaxy made it possible to use x-ray interferometry to determine the profile structure for the system, which was proved correct by x-ray holography. The profile structures established the vectorial orientation of the Ca(2+)-ATPase within these monolayers, to a spatial resolution of approximately 12 A. Such vectorially oriented monolayers of detergent-solubilized Ca(2+)-ATPase from SR make possible a wide variety of correlative structure/function studies, which would serve to elucidate the mechanism of Ca(2+) transport by this enzyme.

Theory of reflectivity of an asymmetric mirror.

By using the concept of transfer matrices and Bloch waves, we have derived a set of equations that provide insight into the operation of asymmetric Bragg reflectors that have been demonstrated to be useful in achieving high reflectivities in strained-material systems. These equations will be useful in the design of asymmetric mirrors and can be used to compare the trade-offs between the conventional, symmetric (quarter-wavelength), and asymmetric mirrors.

Evaluating the effect of co-contraction in optimization models.

The effect of co-contraction of antagonist muscles on spinal compression force is estimated using Karush-Kuhn-Tucker (K-K-T) multipliers. Co-contraction is modelled as an incremental increase in the lower bounds on the allowable muscle forces in an optimization model formation. The K-K-T multipliers associated with each lower bound provide an estimate of the partial derivate of the optimal objective function value with respect to a change in the lower bound. A model whose objective function is spinal compression force is analyzed to estimate the effect of co-contraction on spinal compression force. While the effect depends on the specific muscle and task under consideration, the marginal effect of co-contraction on spinal compression force can be as high as 5.52 N additional spinal compression force for every additional N of muscle force. Paradoxically, the co-contraction may slightly decrease predicted spinal compression in special circumstances.

Vectorially oriented membrane protein monolayers: profile structures via x-ray interferometry/holography.

X-ray interferometry/holography was applied to meridional x-ray diffraction data to determine uniquely the profile structures of a single monolayer of an integral membrane protein and a peripheral membrane protein, each tethered to the surface of a solid inorganic substrate. Bifunctional, organic self-assembled monolayers (SAMs) were utilized to tether the proteins to the surface of Ge/Si multilayer substrates, fabricated by molecular beam epitaxy, to facilitate the interferometric/holographic x-ray structure determination. The peripheral membrane protein yeast cytochrome c was covalently tethered to the surface of a sulfhydryl-terminated 11-siloxyundecanethiol SAM via a disulfide linkage with residue 102. The detergent-solubilized, photosynthetic reaction center integral membrane protein was electrostatically tethered to the surface of an analogous amine-terminated SAM. Optical absorption measurements performed on these two tethered protein monolayer systems were consistent with the x-ray diffraction results indicating the reversible formation of densely packed single monolayers of each fully functional membrane protein on the surface of the respective SAM. The importance of utilizing the organic self-assembled monolayers (as opposed to Langmuir-Blodgett) lies in their ability to tether specifically both soluble peripheral membrane proteins and detergent-solubilized integral membrane proteins. The vectorial orientations of the cytochrome c and the reaction center molecules were readily distinguishable in the profile structure of each monolayer at a spatial resolution of 7 A.

Biomechanical model calculation of muscle contraction forces: a double linear programming method.

This paper presents a novel scheme for the use of linear programming to calculate muscle contraction forces in models describing musculoskeletal system biomechanics. Models of this kind are frequently found in the biomechanics literature. In most cases they involve muscle contraction force calculations that are statically indeterminate, and hence use optimization techniques to make those calculations. We present a linear programming optimization technique that solves a two-objective problem with two sequential linear programs. We use the technique here to minimize muscle intensity and joint compression force, since those are commonly used objectives. The two linear program model has the advantages of low computation cost, ready implementation on a micro-computer, and stable solutions. We show how to solve the model analytically in simple cases. We also discuss the use of the dual problem of linear programming to gain understanding of the solution it provides.

Strained-layer epitaxy of germanium-silicon alloys.

Despite the dominant position of silicon in semiconductor electronics, its use is ultimately limited by its incompatibility with other semiconducting materials. Strained-layer epitaxy overcomes problems of crystallographic compatibility and produces high-quality heterostructures of germanium-silicon layers on silicon. This opens the door to a range of electronic and photonic devices that are based on bandstructure physics.