Protein structure and stability are inherent in the amino acid sequence and governed by non-
covalent interactions. The cooperation between forces is, however, perplexing and not well …

Proteins are the workhorses of life, responsible for catalyzing the numerous chemical
reactions necessary to living cells as well as being important structural molecules. The …

A complete inventory of the forces governing protein folding is critical for productive protein
modeling, including structure prediction and de novo design, as well as understanding …

During the process of protein folding, the amino acid residues along the polypeptide chain
interact with each other in a cooperative manner to form the stable native structure. The …

The focus of this thesis is to understand forces that stabilize proteins. Experiments were
carried out to investigate the degeneracy of sequences that define a protein fold, the effects …

Our ability to predict protein structures from amino acid sequences depends on our
understanding of molecular forces. The same applies to the validation of protein structures …

Protein folding, binding, catalytic activity and molecular recognition all involve molecular
movements, with varying extents. The molecular movements are brought upon via flexible …

Background Regulation of proteins is ubiquitous and vital for any organism. Protein activity
can be altered chemically, by covalent modifications or non-covalent binding of co-factors …

Nature has evolved proteins to counteract forces applied on living cells, and has designed
proteins that can sense forces. One can appreciate Nature's ingenuity in evolving these …

The native structures of proteins result from the balance of intramolecular forces. Each force
is associated with one of the contributions to the free energy, such as electrostatic, van der …