A simple model of globular proteins which incorporates anisotropic attractions is proposed. It is closely related to models used to model simple hydrogen-bonding molecules such as water. Theories for both the fluid and solid phases are presented, and phase diagrams calculated. The model protein exhibits a fluidfluid transition which is metastable with respect to the fluid-solid transition for m...

Protein-surfactant mixtures appear in many industrial and biological applications. Indeed, a fluid as vital as blood contains a mixture of serum albumin proteins with various other smaller surface-active components. Proteins and other surface active molecules are often adsorbed at an air-liquid or liquid-liquid interface due to favorable thermodynamics, and these interfaces play a role in such ...

We present a method to identify all compact, contiguous-chain, structural units in a globular protein from x-ray coordinates. These units are then used to describe a complete set of hierarchic folding pathways for the molecule. Our analysis shows that the larger units are combinations of smaller units, giving rise to a structural hierarchy ranging from the whole protein monomer through supersec...

Vesicles assembled from folded, globular proteins have potential for functions different from traditional lipid or polymeric vesicles. However, they also present challenges in understanding the assembly process and controlling vesicle properties. From detailed investigation of the assembly behavior of recombinant fusion proteins, this work reports a simple strategy to engineer protein vesicles ...

The coil to globule transition of the polypeptide chain is physical phenomenon behind folding globular proteins. Globular proteins with a single domain usually consist about 30 100 amino acid residues, and this finite size extends interval coil-globule phase transition. Based on pedantic derivation two-state model, we introduce number residues as parameter in expressions for two cooperativity m...

Protecting osmolytes are widespread small organic molecules able to stabilize the folded state of most proteins against various denaturing stresses in vivo. The osmophobic model explains thermodynamically their action through a preferential exclusion of the osmolyte molecules from the protein surface, thus favoring the formation of intrapeptide hydrogen bonds. Few works addressed the influence ...

Localization properties of residue fluctuations in globular proteins are studied theoretically by using a Gaussian network model. Participation ratio for each residue fluctuation mode is calculated. It is found that the relationship between participation ratio and frequency is similar for all globular proteins, indicating a universal behavior in spite of their different size, shape, and archite...