Bing Shan

Bing Shan
Bayer HealthCare · Bayer HealthCare Pharmaceuticals

About

16
Publications
560
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447
Citations

Publications

Publications (16)
Article
The rational modification of protein stability is an important goal of protein design. Protein surface electrostatic interactions are not evolutionarily optimized for stability and are an attractive target for the rational redesign of proteins. We show that surface charge mutants can exert stabilizing effects in distinct and unanticipated ways, inc...
Article
Cold denaturation is a general property of globular proteins, but it is difficult to directly characterize since the transition temperature of protein cold denaturation, Tc, is often below the freezing point of water. As a result, studies of protein cold denaturation are often facilitated by addition of denaturants, or by using destabilizing pHs, o...
Article
Full-text available
The interaction between the transactivation domain of p53 (p53TAD) and the N-terminal domain of MDM2 and MDMX plays an essential role for cell function. Mutations in these proteins have been implicated in many forms of cancer. The intrinsically disordered p53TAD contains two subdomains, TAD1 and TAD2. Using NMR spectroscopy, site-directed mutagenes...
Article
Cold denaturation is a general property of globular proteins, and the process provides insight into the origins of the cooperativity of protein folding and the nature of partially folded states. Unfortunately, studies of protein cold denaturation have been hindered by the fact that the cold denatured state is normally difficult to access experiment...
Article
The villin headpiece subdomain, HP36, is the smallest naturally occurring protein that folds cooperatively. Its small size, rapid folding, and simple three-helix topology have made it an extremely popular system for computational studies of protein folding. The role of unfolded state structure in rapid folding is an area of active investigation, bu...
Article
The helical subdomain of the villin headpiece is the smallest naturally occurring cooperatively folded protein. Its small size, simple three-helix topology, and very rapid folding have made it an extremely popular model system for computational and theoretical studies of protein folding. The domain has a well-packed hydrophobic core comprised in pa...
Article
Interest in the structural and dynamic properties of unfolded proteins has increased in recent years owing to continued interest in protein folding and misfolding. Knowledge of the unfolded state under native conditions is particularly important for obtaining a complete picture of the protein folding process. The C-terminal domain of protein L9 is...
Article
The nature of the denatured state ensemble is controversial owing in large part to the difficulty of characterizing the structure and energetics of denatured state interactions. Denatured states can be populated under a variety of extreme conditions but the state which is most relevant for protein folding and engineering is the denatured state ense...
Article
There is considerable interest in the properties of the unfolded states of proteins, particularly unfolded states which can be populated in the absence of high concentrations of denaturants. Interest in the unfolded state ensemble reflects the fact that it is the starting point for protein folding as well as the reference state for protein stabilit...
Article
A hyperstable variant of the small independently folded helical subdomain (HP36) derived from the F-actin binding villin headpiece was designed by targeting surface electrostatic interactions and helical propensity. A double mutant N68A, K70M was significantly more stable than wild type. The Tm of wild type in aqueous buffer is 73.0 degrees C, wher...
Article
A point mutation of a small globular protein, the C-terminal domain of L9 destabilizes the protein and leads to observable cold-denaturation at temperatures above zero. The cold denatured state is in slow exchange with the native state on the NMR time scale, and this allows the hydrodynamic properties of the cold unfolded state and the native state...
Article
Ozone-induced grafting was developed to improve the hemocompatibility of biomaterials based on low-density polyethylene (LDPE). An LDPE film was activated with ozone and graft-polymerized with N,N′-dimethyl(methacryloylethyl)ammonium propane sulfonate (DMAPS). The existence of sulfobetaine structures on the grafted film was confirmed by X-ray photo...
Article
Ozonization, a novel surface modification method, has been developed to improve hemocompatibility of polymeric biomaterials. The silicone film was exposed to ozone and then followed by grafted polymerization with 2-methacryloyloxyethyl phosphorylcholine (MPC). The surface graft polymerization was confirmed by X-ray photon spectroscopy and ATR-FTIR....
Article
2‐Methacryloyloxyethyl phosphorylcholine (MPCE) was synthesized using phosphorus trichloride, ethylene glycol, 2‐hydroxyethyl methacrylate and triethylamine, and then used in the preparation of O ‐butyrylchitosan‐bonded MPCE (MPCE–BCS) by Michael addition of MPCE to amino groups of O ‐butyrylchitosan. The structures of MPCE and MPCE–BCS were charac...

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