Conformational flexibility of a model protein upon immobilization on self‐assembled monolayers

Tiwari

et al. 2013

IJMS

387

195

Enzymes found in nature have been exploited in industry due to their inherent catalytic properties in complex chemical processes under mild experimental and environmental conditions. The desired industrial goal is often difficult to achieve using the native form of the enzyme. Recent developments in protein engineering have revolutionized the development of commercially available enzymes into better industrial catalysts. Protein engineering aims at modifying the sequence of a protein, and hence its structure, to create enzymes with improved functional properties such as stability, specific activity, inhibition by reaction products, and selectivity towards non-natural substrates. Soluble enzymes are often immobilized onto solid insoluble supports to be reused in continuous processes and to facilitate the economical recovery of the enzyme after the reaction without any significant loss to its biochemical properties. Immobilization confers considerable stability towards temperature variations and organic solvents. Multipoint and multisubunit covalent attachments of enzymes on appropriately functionalized supports via linkers provide rigidity to the immobilized enzyme structure, ultimately resulting in improved enzyme stability. Protein engineering and immobilization techniques are sequential and compatible approaches for the improvement of enzyme properties. The present review highlights and summarizes various studies that have aimed to improve the biochemical properties of industrially significant enzymes.

Section: Immobilization To Upgrade Industrial Enzymesmentioning

confidence: 99%

From Protein Engineering to Immobilization: Promising Strategies for the Upgrade of Industrial Enzymes

Tiwari

et al. 2013

IJMS

387

195

“…These fine effects are conveyed throughout the protein structure via subtle local conformational changes that are brought by the presence of specific ligands; in other words, it is the environment of the allosteric protein that is regulating its function [85]. Allostery may be an intrinsic property of all proteins [86], and structural flexibility is important for all protein functions [87].…”

Section: Effect Of Ligandsmentioning

confidence: 99%

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Ebrahim‐Habibi

Morshedi

Rezaei‐Ghaleh

et al. 2010

JICS

Protein aggregates, whether amorphous or structured (amyloid), have attracted much attention in recent years and despite extensive efforts, the mechanism of their formation is poorly understood. While "natural" aggregation (polymerization) of monomers could improve the biological function of some proteins, it is usually the darker side of this phenomenon which is discussed in many studies: deleterious aggregation that could lead to loss of biological activity under in vitro conditions or cause misfolding diseases. In this review, protein aggregation has been overviewed, starting from some general concepts involved in its formation, followed by mentioning studies aimed at elucidation of its kinetics and mechanism, or characterization of intermediates that would be aggregation-prone, and finally, reporting some of the studies related to the design of methods that would control the process. Similarly, amyloid aggregates have been defined, and current methods used in their characterization have been briefly described, with an emphasis on in silico studies. Finally, identification and design of such molecules which may be effective in control of this process is discussed.

“…Γ ≫ 1 without pair contribution Although it has been less studied than its like-charge counterpart [1][2][3], the behaviour of two interacting oppositely charged mesoscopic bodies in solution is of importance in various contexts, including colloid physics [4][5][6][7][8], biochemistry related experiment interpretations [9,10], drug design [11], and structural biology [12]. The simple system of two charged plates with opposite uniform surface charges represents a model of choice that enables one to get analytical results in some limits, and furthermore, that provides a starting point to estimate the interaction energy between two colloids of various geometry [13,14].…”

Section: Introductionmentioning

confidence: 99%

Interaction regimes for oppositely charged plates with multivalent counterions

Paillusson

Trizac

2011

Phys. Rev. E

Within a mean-field treatment of the interaction between two oppositely charged plates in a salt-free solution, the distance at which a transition from an attractive to a repulsive regime appears can be computed analytically. The mean-field description, however, breaks down under strong Coulombic couplings, which can be achieved at room temperature with multivalent counterions and highly charged surfaces. Making use of the contact theorem and simple physical arguments, we propose explicit expressions for the equation of state in several situations at short distances. The possibility of Bjerrum pair formation is addressed and is shown to have profound consequences on the interactions. To complete the picture, we consider the large-distance limit, from which schematic phase diagram discriminating attractive from repulsive regions can be proposed.