Fusarium solani pisi cutinase
MR Egmond, J de Vlieg - Biochimie, 2000 - Elsevier
Cutinase from Fusarium solani pisi has been studied extensively with respect to its structural
and functional properties. The crystal structure of the enzyme was solved to high atomic …
and functional properties. The crystal structure of the enzyme was solved to high atomic …
Isolation of lipids from biological samples
Isolation of the lipid fraction from biological samples has been a crucial part of countless
studies over the last century. This considerable research interest has led to the development of …
studies over the last century. This considerable research interest has led to the development of …
Incorporating ECE-pincer metal complexes as functional building blocks in semisynthetic metalloenzymes, supramolecular polypeptide hybrids, tamoxifen derivatives …
B Wieczorek, HP Dijkstra, MR Egmond… - Journal of …, 2009 - Elsevier
ECE-pincer metal compounds often have excellent thermal and chemical stability, which
makes these organometallics attractive for use as building blocks in bioorganometallic …
makes these organometallics attractive for use as building blocks in bioorganometallic …
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
The family of lipases (triacylglycerol-acyl-hydrolases, EC 3.1.1.3) constitutes an interesting
class of enzymes because of their ability to interact with lipid-water interfaces, their wide …
class of enzymes because of their ability to interact with lipid-water interfaces, their wide …
Structural evidence for dimerization-regulated activation of an integral membrane phospholipase
HJ Snijder, I Ubarretxena-Belandia, M Blaauw, KH Kalk… - Nature, 1999 - nature.com
Dimerization is a biological regulatory mechanism employed by both soluble and membrane
proteins 1 . However, there are few structural data on the factors that govern dimerization of …
proteins 1 . However, there are few structural data on the factors that govern dimerization of …
[HTML][HTML] Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
L Vandeputte‐Rutten, RA Kramer, J Kroon… - The EMBO …, 2001 - embopress.org
OmpT from Escherichia coli belongs to a family of highly homologous outer membrane
proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram‐…
proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram‐…
Crystal structure of the copper-containing quercetin 2, 3-dioxygenase from Aspergillus japonicus
F Fusetti, KH Schröter, RA Steiner, PI van Noort… - Structure, 2002 - cell.com
Quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of
molecular oxygen into polyphenolic flavonols. Dioxygenation catalyzed by iron-containing …
molecular oxygen into polyphenolic flavonols. Dioxygenation catalyzed by iron-containing …
Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air− water interface
PA Wierenga, MBJ Meinders, MR Egmond… - Langmuir, 2003 - ACS Publications
Using native and caprylated ovalbumin, the role of exposed hydrophobicity on the kinetics
of protein adsorption to the air−water interface is studied. First, changes in the chemical …
of protein adsorption to the air−water interface is studied. First, changes in the chemical …
Quantitative description of the relation between protein net charge and protein adsorption to air− water interfaces
PA Wierenga, MBJ Meinders, MR Egmond… - The Journal of …, 2005 - ACS Publications
In this study a set of chemically engineered variants of ovalbumin was produced to study the
effects of electrostatic charge on the adsorption kinetics and resulting surface pressure at …
effects of electrostatic charge on the adsorption kinetics and resulting surface pressure at …
In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT
RA Kramer, D Zandwijken… - European journal of …, 2000 - Wiley Online Library
OmpT is a protease present in the outer membrane of Escherichia coli. The enzyme was
overexpressed without its signal sequence in E. coli using a T7 system, resulting in the …
overexpressed without its signal sequence in E. coli using a T7 system, resulting in the …