Single-Molecule Fluorescence Studies of Protein Folding and Conformational Dynamics

Single-molecule fluorescence studies of protein folding and conformational dynamics.

Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones

Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases. Protein folding is a highly heterogeneous process and rarely populated intermediate states may play an important role. Single-molecule techniques are ideally suited to resolve these heterogeneities. In this thesis, I ...

Single Molecule Fluorescence Investigation of Protein Folding

Title of Document: SINGLE MOLECULE FLUORESCENCE INVESTIGATION OF PROTEIN FOLDING Jianwei Liu, Ph.D., 2008 Directed By: Associate Professor, Victor Muñoz, Department of Chemistry and Biochemistry In addition to the well known two-state folding scenario, the energy landscape theory of protein folding predicts the possibility of downhill folding under native conditions. This intriguing prediction ...

Single-molecule fluorescence spectroscopy of protein folding.

Single-molecule spectroscopy is an important new approach for studying the intrinsically heterogeneous process of protein folding. This Review illustrates how different single-molecule fluorescence techniques have improved our understanding of mechanistic aspects in protein folding, exemplified by a series of recent experiments on a small protein.

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...