The application of single-chain Fv fragments (scFv) in medicine and biotechnology places
great demands on their stability. Only recently has attention been given to the production of …

An understanding of the forces that contribute to stability is pivotal in solving the protein‐
folding problem. Classical theory suggests that disulfide bonds stabilize proteins by …

Protein solubility is a problem for many protein chemists, including structural biologists and
developers of protein pharmaceuticals. Knowledge about how intrinsic factors influence …

Production of recombinant proteins in bacteria is limited by the formation of cytoplasmic
aggregates (inclusion bodies or “IBs”). This review summarizes what is known about why IBs …

Proteins carry out the most difficult tasks in living cells. They do so by interacting specifically
with other molecules. This requires that they fold to a unique, globular conformation that is …

There are great demands on the stability, expression yield and resistance to aggregation of
antibody fragments. To untangle intrinsic domain effects from domain interactions, we …

Referee: Dr. Ruth Nussinov, Saic Frederick, Bldg. 469. 469, Room 151, Frederick, MD
21702-1201 Hyperthermophilic organisms optimally grow close to the boiling point of water …

The sol‐gel method of encapsulating proteins in a silica matrix was investigated as a
potential experimental system for testing the effects of molecular confinement on the …

Control and prevention of unwanted aggregation for therapeutic proteins is a ubiquitous
hurdle during biopharmaceutical product manufacture, storage, shipping, and …

The net charge and isoelectric pH (pI) of a protein depend on the content of ionizable groups
and their pK values. Ribonuclease Sa (RNase Sa) is an acidic protein with a pI= 3.5 that …