Protein structures in nature often exhibit a high degree of regularity (for example, secondary
structure and tertiary symmetries) that is absent from random compact conformations. With …

Presenting a wide-ranging view of current developments in protein research, the papers in
this collection, each written by highly regarded experts in the field, examine various aspects …

1. THE PROTEIN FOLDING PROBLEM To be biologically active, all proteins must adopt
specific folded three-dimensional structures. Yet the genetic information for the protein …

Publisher Summary This chapter provides an insight that quantitative predictions of the
stability and cooperative folding behavior of proteins are within reach. The problem of …

Experiment and simulation are now conspiring to give atomic-level descriptions of protein
folding relevant to folding, misfolding, trafficking, and degradation in the cell. We are on the …

Thanks to incisive studies over many years, much has been learned of the interactions that
stabilize folded proteins (1-4). The advent of directed mutagenesis has made it possible to …

Protein function arises from a poorly understood pattern of energetic interactions between
amino acid residues. Sequence-based strategies for deducing this pattern have been …

The functional properties of food proteins affect behavior in food systems and influence the
quality attributes, structure, texture, mouth-feel, and flavor of the final product. These …

A major factor in the folding of proteins is the burying of hydro-phobic side chains. A specific
example is the packing of α-helices on β-sheets by interdigitation of nonpolar side chains …

D-Galactose-binding (or chemoreceptor) protein of Escherichia coli serves as an initial
component for both chemotaxis towards galactose and glucose and high-affinity active …