Studies of Protein Folding in Wright/Dyson Laboratory

Computational studies of protein folding

These polymers, comprised of 20 naturally occurring amino acids, fold to a unique, biologically active conformation called the native state. Various genome-sequencing projects now list the parts of such protein sequences in a given organism, but unfortunately, this list is of little utility; the real need is to identify the functions of all these proteins, which range from molecular to physiolo...

Computational studies of protein folding

NMR studies of protein folding

NMR spectroscopy is the method of choice for determining the structural details of unfolded and partially folded states of proteins. Here, the utility of NMR spectroscopy in characterizing such disordered states which populate protein folding pathways, is discussed. The relevance of the structural information obtained to protein folding mechanisms is examined critically. NMR spectroscopy can no...

Mass spectrometry studies of protein folding

Mass spectrometry has become a powerful method to study the structure and dynamics of proteins. Hydrogen/deuterium exchange in conjunction with mass spectrometry is now becoming more widely used to monitor conformational changes in proteins, and when combined with proteolytic digestion or gas-phase dissociation, it can provide spatial resolution of structural regions which participate in confor...

Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions

Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...