Protein design: From the aspect of water solubility and stability
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 …
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 …
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
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 …
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
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 …
rationalization. The desolvation effects and intra‐protein interactions, which cause variations …
Chemistry and enzymology of disulfide cross-linking in proteins
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 …
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 …
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 …
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 …
This journal offers authors two options (open access or subscription) to publish research …
Structure, function, and mechanism of thioredoxin proteins
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 …
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 …
that are otherwise undetectable, and perhaps suggest unsuspected functional properties. In …