Spectrophotometric study of the interaction of tetraphenylporphyrin tetrasulfonate (TPPS4) with proteins

The interaction of water-soluble porphyrin TPPS(4) (tetraphenylporphyrin tetrasulfonate) with proteins in acidic solution was studied by spectrophotometry. The absorption spectra of TPPS(4)-protein complexes, the aggregation of TPPS(4) in acidic solution, and comparison of the absorption spectra of TPPS(4)-protein conjugate with that of the TPPS(4)-protein complex was investigated in detail. The effects of denaturants including urea and SDS were also examined. A mechanism was proposed that TPPS(4) would be distributed between microphase of protein and the aqueous solution and then aggregated in the microphase.     

Systematic quantification of the dynamics of newly synthesized proteins unveiling their degradation pathways in human cells

Proteins are continuously synthesized during cell growth and proliferation. At the same time, excessive and misfolded proteins have to be degraded, otherwise they are a burden to cells. Protein degradation is essential to maintain proteostasis in cells, and dysfunction of protein degradation systems results in numerous diseases such as cancer and neurodegenerative diseases. Despite the importance of protein degradation, the degradation pathways of many proteins remain to be explored. Here, we comprehensively investigated the degradation of newly synthesized proteins in human cells by integrating metabolic labeling, click chemistry, and multiplexed proteomics, and systematic and quantitative analysis of newly synthesized proteins first revealed the degradation pathways of many proteins. Bioinformatic analysis demonstrates that proteins degraded through two major pathways have distinct properties and functions. Proteins degraded through the ubiquitin-proteasome pathway contain more disordered structures, whereas those through the autophagy-lysosome pathway have significantly higher hydrophobicity. Systematic and quantitative investigation of the dynamics of newly synthesized proteins provides unprecedented and valuable information about protein degradation, which leads to a better understanding of protein properties and cellular activities.

Systematic quantification of the dynamics of newly synthesized proteins first reveals the degradation pathways of many proteins in human cells, and proteins degraded through each of the two major pathways have distinct properties and functions.     

Limits of One-dimensional Interacting Particle Systems with Two-scale Interaction*

This paper characterizes the limits of a large system of interacting particles distributed on the real line. The interaction occurring among neighbors involves two kinds of independent actions with different rates. This system is a generalization of the voter process, of which each particle is of type A or a. Under suitable scaling, the local proportion functions of A particles converge to continuous functions which solve a class of stochastic partial differential equations driven by Fisher-Wrig...     

An identification of the connections of Quillen and Beilinson-Schechtman

Given a family of Riemann surfaces and a holomorphic vector bundle Beilinson and Schechtman construct a canonical connection on the associated determinant bundle. We prove the conjecture which states that their connection coincides with the Quillen connection. This is done by reducing to the case where along fibers are invertible. Both connection forms become more accessible in this case.Supported in part by N.S.F. Grant No. DMS-9201022Supported in part by National Science Council of Republic of China Grant No. NSC 82-0208-M-002-125-T, and NSERC of Canada Grant No. OGP 0121883     

Mechanism of lamellar spacing adjustment in directionally frozen agar gels

A theory is presented for predicting the size of ice crystals which result from steady-state, unidirectional growth within aqueous agar gels. Cellular arrays of adjacent ice crystals were separated by an amorphous water-agar membrane at a composition near the vitrification point. Using this vitrification composition and both a steady-state condition and a minimum free energy criterion, the size of ice crystals was predicted for a given solidification velocity and diffusion condition. It was found, however, that this simple model could not predict the trend towards larger crystal sizes that was observed when the initial agar concentration in the gels increased from 3% to 10% by weight agar.