Protein design: From the aspect of water solubility and stability

R Qing, S Hao, E Smorodina, D Jin, A Zalevsky… - Chemical …, 2022 - ACS Publications
Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications

CL Young, ZT Britton, AS Robinson - Biotechnology journal, 2012 - Wiley Online Library
Protein fusion tags are indispensible tools used to improve recombinant protein expression
yields, enable protein purification, and accelerate the characterization of protein structure …

Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily

D Sheehan, G Meade, VM Foley… - Biochemical journal, 2001 - portlandpress.com
The glutathione transferases (GSTs; also known as glutathione S-transferases) are major
phase II detoxification enzymes found mainly in the cytosol. In addition to their role in …

Very fast empirical prediction and rationalization of protein pKa values

H Li, AD Robertson, JH Jensen - Proteins: Structure, Function …, 2005 - Wiley Online Library
A very fast empirical method is presented for structure‐based protein pKa prediction and
rationalization. The desolvation effects and intra‐protein interactions, which cause variations …

Chemistry and enzymology of disulfide cross-linking in proteins

D Fass, C Thorpe - Chemical reviews, 2018 - ACS Publications
Cysteine thiols are among the most reactive functional groups in proteins, and their pairing
in disulfide linkages is a common post-translational modification in proteins entering the …

Formation and transfer of disulphide bonds in living cells

CS Sevier, CA Kaiser - Nature reviews Molecular cell biology, 2002 - nature.com
Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

Protein disulfide isomerase

B Wilkinson, HF Gilbert - Biochimica et biophysica acta (BBA)-proteins and …, 2004 - Elsevier
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link
specific cysteines are often added to stabilize a protein or to join it covalently to other …

Thioredoxin—a fold for all reasons

JL Martin - Structure, 1995 - cell.com
Thioredoxin —a fold for all reasons: Structure Skip to Main Content Advertisement Structure
This journal offers authors two options (open access or subscription) to publish research …

Structure, function, and mechanism of thioredoxin proteins

JF Collet, J Messens - Antioxidants & redox signaling, 2010 - liebertpub.com
Thioredoxins are ubiquitous antioxidant enzymes that play important roles in many health-
related cellular processes. As such, the fundamental knowledge of how these enzymes work …

Surprising similarities in structure comparison

JF Gibrat, T Madej, SH Bryant - Current opinion in structural biology, 1996 - Elsevier
Examination of a protein's structural 'neighbors' can reveal distant evolutionary relationships
that are otherwise undetectable, and perhaps suggest unsuspected functional properties. In …