Protein stabilization was achieved through in vivo screening based on the thermodynamic
linkage between protein folding and fragment complementation. The split GFP system was …

In this paper we describe the evolution of eCGP123, an extremely stable green fluorescent
protein based on a previously described fluorescent protein created by consensus …

In this study, we aim to relate experimentally measured macroscopic properties to dynamic
and structural changes as calculated by molecular dynamics (MD) simulations. We …

Folding of the Protein G B1 domain (PGB1) shifts with increasing salt concentration from a
cooperative assembly of inherently unstructured subdomains to an assembly of partly pre …

Truncated green fluorescent protein (GFP) that is refolded after removing the 10th β-strand
can readily bind to a synthetic strand to recover the absorbance and fluorescence of the …

Fluorescence resonance energy transfer (FRET) was used to establish a novel in vivo
screening system that allows rapid detection of protein folding and protein variants with …

Stability of green fluorescent protein (GFP) is sometimes important for a proper practical
application of this protein. Random mutagenesis and targeted mutagenesis have been used …

Many green fluorescent protein (GFP) variants have been developed for use as fluorescent
tags, and recently a superfolder GFP (sfGFP) has been developed as a robust folding …

Information about the stability of proteins is paramount to determine their optimal storage or
reaction conditions. It is also essential to determine protein stability in high-throughput when …

Overproduction of soluble and stable proteins for functional and structural studies is a major
bottleneck for structural genomics programs and traditional biochemistry laboratories. Many …