Publisher Summary This chapter deals with the structure of the molten globules of various
globular proteins revealed by the recent experimental studies. Recent advances in …

▪ Abstract Most experimental studies on the dynamics of protein folding have been confined
to timescales of 1 ms and longer. Yet it is obvious that many phenomena that are obligatory …

Vibrational dynamics of folded proteins is studied using a Gaussian model in which the
protein is viewed as a network, residues representing the junctions, and the connectivity …

A predictive rule for protein folding is presented that involves two recurrent glycine-based
motifs that cap the carboxyl termini of α helices. In proteins, helices that terminated in glycine …

A physical theory of protein secondary structure is proposed and tested by performing
exceedingly simple Monte Carlo simulations. In essence, secondary structure propensities …

Multi-dimensional heteronuclear NMR spectroscopy has been used to obtain structural
information on isotopically labeled recombinant sperm whale apomyoglobin in the native …

The specific function of a protein is determined by its structure and the ability of the structure
to evolve with time. The functional three-dimensional structure is generally determined by …

We report the fast relaxation dynamics of “native” apomyoglobin (pH 5.3) following a 10-ns,
laser-induced temperature jump. The structural dynamics are probed using time-resolved …

We describe LINUS, a hierarchic procedure to predict the fold of a protein from its amino
acid sequence alone. The algorithm, which has been implemented in a computer program …

Globular proteins often exhibit cooperative unfolding transitions in which only folded (native)
and unfolded (denatured) molecules are populated at equilibrium. 1, 2 This two-state …