Protein sequence and structure: Is one more fundamental than the other?

We argue that protein native state structures reside in a novel "phase" of matter which confers on proteins their many amazing characteristics. This phase arises from the common features of all globular proteins and is characterized by a sequence-independent free energy landscape with relatively few low energy minima with funnel-like character. The choice of a sequence that fits well into one of these predetermined structures facilitates rapid and cooperative folding. Our model calculations show that this novel phase facilitates the formation of an efficient route for sequence design starting from random peptides.Comment: 7 pages, 4 figures, to appear in J. Stat. Phy

Ground-state properties of tubelike flexible polymers

In this work we investigate structural properties of native states of a simple model for short flexible homopolymers, where the steric influence of monomeric side chains is effectively introduced by a thickness constraint. This geometric constraint is implemented through the concept of the global radius of curvature and affects the conformational topology of ground-state structures. A systematic analysis allows for a thickness-dependent classification of the dominant ground-state topologies. It turns out that helical structures, strands, rings, and coils are natural, intrinsic geometries of such tubelike objects

Rigorous analytical modeling of high-aperture focusing through a spherical interface

10.1364/JOSAA.30.001426Journal of the Optical Society of America A: Optics and Image Science, and Vision3071426-1440JOAO

Multipole theory for tight focusing of polarized light, including radially polarized and other special cases

Journal of the Optical Society of America A: Optics and Image Science, and Vision29132-43JOAO

Multipole and plane wave expansions of diverging and converging fields

10.1364/OE.22.008949Optics Express2288949-896