Search Results - "van Mierlo, Carlo P."

Mechanism of the small ATP-independent chaperone Spy is substrate specific by Mitra, Rishav, Gadkari, Varun V., Meinen, Ben A., van Mierlo, Carlo P. M., Ruotolo, Brandon T., Bardwell, James C. A.

“…ATP-independent chaperones are usually considered to be holdases that rapidly bind to non-native states of substrate proteins and prevent their aggregation…”
Get full text

Fluorescence of Alexa fluor dye tracks protein folding by Lindhoud, Simon, Westphal, Adrie H, Visser, Antonie J W G, Borst, Jan Willem, van Mierlo, Carlo P M

“…Fluorescence spectroscopy is an important tool for the characterization of protein folding. Often, a protein is labeled with appropriate fluorescent donor and…”
Get full text

Cofactor binding protects flavodoxin against oxidative stress by Lindhoud, Simon, van den Berg, Willy A M, van den Heuvel, Robert H H, Heck, Albert J R, van Mierlo, Carlo P M, van Berkel, Willem J H

“…In organisms, various protective mechanisms against oxidative damaging of proteins exist. Here, we show that cofactor binding is among these mechanisms,…”
Get full text

The Arabidopsis thaliana SERK1 kinase domain spontaneously refolds to an active state in vitro by Aan den Toorn, Marije, Huijbers, Mieke M E, de Vries, Sacco C, van Mierlo, Carlo P M

“…Auto-phosphorylating kinase activity of plant leucine-rich-repeat receptor-like kinases (LRR-RLK's) needs to be under tight negative control to avoid…”
Get full text

Molecular Dynamics Study of the Solvation of an α-Helical Transmembrane Peptide by DMSO by Duarte, Afonso M. S, van Mierlo, Carlo P. M, Hemminga, Marcus A

“…A 10-ns molecular dynamics study of the solvation of a hydrophobic transmembrane helical peptide in dimethyl sulfoxide (DMSO) is presented. The objective is to…”
Get full text

The Folding Energy Landscape of Apoflavodoxin Is Rugged: Hydrogen Exchange Reveals Nonproductive Misfolded Intermediates by Bollen, Yves J. M., Kamphuis, Monique B., van Mierlo, Carlo P. M.

“…Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and NMR spectroscopy. Knowledge…”
Get full text

Conformation and Orientation of a Protein Folding Intermediate Trapped by Adsorption by Maarten F. M. Engel, Antonie J. W. G. Visser, Carlo P. M. van Mierlo, Frieden, Carl

“…Although adsorption-induced conformational changes of proteins play an essential role during protein adsorption on interfaces, detailed information about these…”
Get full text

Folding of proteins with a flavodoxin‐like architecture by Houwman, Joseline A., Mierlo, Carlo P. M.

“…The flavodoxin‐like fold is a protein architecture that can be traced back to the universal ancestor of the three kingdoms of life. Many proteins share this…”
Get full text

Reversible Temperature-Switching of Hydrogel Stiffness of Coassembled, Silk-Collagen-Like Hydrogels by Rombouts, Wolf H, de Kort, Daan W, Pham, Thao T. H, van Mierlo, Carlo P. M, Werten, Marc W. T, de Wolf, Frits A, van der Gucht, Jasper

“…Recombinant protein polymers, which can combine different bioinspired self-assembly motifs in a well-defined block sequence, have large potential as building…”
Get full text

Double Electron–Electron Spin Resonance Tracks Flavodoxin Folding by van Son, Martin, Lindhoud, Simon, van der Wild, Matthijs, van Mierlo, Carlo P. M, Huber, Martina

“…Protein folding is one of the important challenges in biochemistry. Understanding the folding process requires mapping of protein structure as it folds. Here…”
Get full text

Concurrent presence of on- and off-pathway folding intermediates of apoflavodoxin at physiological ionic strength by Houwman, Joseline A, Westphal, Adrie H, Visser, Antonie J W G, Borst, Jan Willem, van Mierlo, Carlo P M

“…Flavodoxins have a protein topology that can be traced back to the universal ancestor of the three kingdoms of life. Proteins with this type of architecture…”
Get more information

Multiple Steps during the Formation of β-Lactoglobulin Fibrils by Arnaudov, Luben N, de Vries, Renko, Ippel, Hans, van Mierlo, Carlo P. M

“…In this study, the heat induced fibrilar aggregation of the whey protein β-lactoglobulin is investigated at low pH and at low ionic strength. Under these…”
Get full text

Extensive Formation of Off-Pathway Species during Folding of an α−β Parallel Protein Is Due to Docking of (Non)native Structure Elements in Unfolded Molecules by Nabuurs, Sanne M, Westphal, Adrie H, van Mierlo, Carlo P. M

“…Detailed information about unfolded states is required to understand how proteins fold. Knowledge about folding intermediates formed subsequently is essential…”
Get full text

A General Approach for Detecting Folding Intermediates from Steady-State and Time-Resolved Fluorescence of Single-Tryptophan-Containing Proteins by Laptenok, Sergey P, Visser, Nina V, Engel, Ruchira, Westphal, Adrie H, van Hoek, Arie, van Mierlo, Carlo P. M, van Stokkum, Ivo H. M, van Amerongen, Herbert, Visser, Antonie J. W. G

“…During denaturant-induced equilibrium (un)folding of wild-type apoflavodoxin from Azotobacter vinelandii, a molten globule-like folding intermediate is formed…”
Get full text

Noncooperative Formation of the Off-Pathway Molten Globule during Folding of the α−β Parallel Protein Apoflavodoxin by Nabuurs, Sanne M, Westphal, Adrie H, van Mierlo, Carlo P. M

“…During folding of many proteins, molten globules are formed. These partially folded forms of proteins have a substantial amount of secondary structure but lack…”
Get full text

Rise-time of FRET-acceptor fluorescence tracks protein folding by Lindhoud, Simon, Westphal, Adrie H, van Mierlo, Carlo P M, Visser, Antonie J W G, Borst, Jan Willem

“…Uniform labeling of proteins with fluorescent donor and acceptor dyes with an equimolar ratio is paramount for accurate determination of Förster resonance…”
Get full text

Macromolecular Crowding Compacts Unfolded Apoflavodoxin and Causes Severe Aggregation of the Off-pathway Intermediate during Apoflavodoxin Folding by Engel, Ruchira, Westphal, Adrie H., Huberts, Daphne H.E.W., Nabuurs, Sanne M., Lindhoud, Simon, Visser, Antonie J.W.G., van Mierlo, Carlo P.M.

“…To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding. Here, the influence of…”
Get full text

Topological Switching between an α−β Parallel Protein and a Remarkably Helical Molten Globule by Nabuurs, Sanne M, Westphal, Adrie H, aan den Toorn, Marije, Lindhoud, Simon, van Mierlo, Carlo P. M

“…Partially folded protein species transiently exist during folding of most proteins. Often these species are molten globules, which may be on- or off-pathway to…”
Get full text

Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein by Lindhoud, Simon, Westphal, Adrie H, Borst, Jan Willem, van Mierlo, Carlo P M

“…Partially folded protein species transiently form during folding of most proteins. Often, these species are molten globules, which may be on- or off-pathway to…”
Get full text

Formation of On- and Off-Pathway Intermediates in the Folding Kinetics of Azotobacter vinelandii Apoflavodoxin by Bollen, Yves J. M, Sánchez, Ignacio E, van Mierlo, Carlo P. M

“…The folding kinetics of the 179-residue Azotobacter vinelandii apoflavodoxin, which has an α−β parallel topology, have been followed by stopped-flow…”
Get full text