Protein design: toward functional metalloenzymes

F Yu, VM Cangelosi, ML Zastrow, M Tegoni… - Chemical …, 2014 - ACS Publications
Protein design is a valuable tool for understanding the fundamental factors that dictate
protein structure and function. The field of protein design has seen significant progress over …

The application of circular dichroism to studies of protein folding and unfolding

SM Kelly, NC Price - Biochimica et Biophysica Acta (BBA)-Protein Structure …, 1997 - Elsevier
In this review, we shall outline the basic principles Ž. of circular dichroism CD and indicate
the types of structural information relevant to the study of the Ž. folding and unfolding or …

Small-molecule hydrophobic tagging–induced degradation of HaloTag fusion proteins

TK Neklesa, HS Tae, AR Schneekloth… - Nature chemical …, 2011 - nature.com
The ability to regulate any protein of interest in living systems with small molecules remains
a challenge. We hypothesized that appending a hydrophobic moiety to the surface of a …

Heterogeneity in protein folding and unfolding reactions

S Bhatia, JB Udgaonkar - Chemical Reviews, 2022 - ACS Publications
Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

[HTML][HTML] Understanding protein folding via free-energy surfaces from theory and experiment

AR Dinner, A Šali, LJ Smith, CM Dobson… - Trends in biochemical …, 2000 - cell.com
The ability of protein molecules to fold into their highly structured functional states is one of
the most remarkable evolutionary achievements of biology. In recent years, our …

Assessing protein disorder and induced folding

V Receveur‐Bréchot, JM Bourhis… - Proteins: Structure …, 2006 - Wiley Online Library
Intrinsically disordered proteins (IDPs) defy the structure–function paradigm as they fulfill
essential biological functions while lacking well‐defined secondary and tertiary structures …

Protein folding intermediates and pathways studied by hydrogen exchange

SW Englander - Annual review of biophysics and biomolecular …, 2000 - annualreviews.org
▪ Abstract In order to solve the immensely difficult protein-folding problem, it will be
necessary to characterize the barriers that slow folding and the intermediate structures that …

Mass spectrometry-based fast photochemical oxidation of proteins (FPOP) for higher order structure characterization

KS Li, L Shi, ML Gross - Accounts of chemical research, 2018 - ACS Publications
Conspectus Assessment of protein structure and interaction is crucial for understanding
protein structure/function relationships. Compared to high-resolution structural tools …

Kinetic role of early intermediates in protein folding

H Roder, W Colón - Current opinion in structural biology, 1997 - Elsevier
The traditional view that partly folded intermediates are important for directing a protein
toward the native state has been challenged by the notion that proteins can intrinsically fold …

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

P Goloubinoff, AS Sassi, B Fauvet, A Barducci… - Nature chemical …, 2018 - nature.com
During and after protein translation, molecular chaperones require ATP hydrolysis to favor
the native folding of their substrates and, under stress, to avoid aggregation and revert …