Includes bibliographical references and index.
|Statement||Yoshiaki Nosoh, Takeshi Sekiguchi.|
|Series||Ellis Horwood series in biochemistry and biotechnology|
|Contributions||Sekiguchi, Takeshi, 1945-|
|LC Classifications||TP248.65.P76 N67 1991|
|The Physical Object|
|Pagination||223 p. :|
|Number of Pages||223|
|LC Control Number||91033063|
Stability has been the major target for protein engineering, mainly to increase thermal stability [1, 2], but sometimes also to destabilize proteins . Effects on stability have been. Integral membrane proteins (IMPs) are crucial components of all cells but are difficult to study in vitro because they are generally unstable when removed from their native membranes using detergents. Despite the major biomedical relevance of IMPs, less than 1% of Protein Data Bank (PDB) entries are IMP structures, reflecting the technical gap between studies of soluble proteins compared to by: This article defines protein stability, emphasizes its importance and surveys some notable recent publications (–) in the field of protein stability/stabilization. Knowledge of the factors stabilizing proteins has emerged from denaturation studies and from study of thermophilic (and other extremophilic) by: pare the protein engineering methods that have been applied to ﬁnd sequence modiﬁcations that confer increased IMP stability without disrupting bio-logical functionality. Stabilized IMPs through mutations Pioneering work in the membrane protein stabilization ﬁeld was carried out .
Protein stability is often a limiting factor in the development of commercial proteins and biopharmaceuticals, as well as for biochemical and structural studies. Unfortunately, identifying Cited by: Stabilization of a strained protein loop conformation through protein engineering Article in Protein Science 4(3) March with 28 Reads How we measure 'reads'. 1. Protein Sci. Mar;4(3) Stabilization of a strained protein loop conformation through protein engineering. Hodel A(1), Kautz RA, Fox RO. Author information: (1)Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut , by: 9. The route to engineering stability of a protein of interest lies largely with the available data. Where high-resolution structural data is available, rational design, based on fundamental principles of protein chemistry, can improve protein by: 1.
Polymerization of this protein produces a chain of protein subunits, each of which bears a shallow knot, yet the continuous path through the polymer backbone is unknotted (Fig. 1b). This polymer served as a control, and allowed a direct assessment of the effects knot depth and complex topology have on the properties of the by: The accurate prediction of the impact of an amino acid substitution on the thermal stability of a protein is a central issue in protein science, and is of key relevance for the rational Cited by: Protein engineering is the process of developing useful or valuable is a young discipline, with much research taking place into the understanding of protein folding and recognition for protein design principles. It is also a product and services market, with an estimated value of $ billion by However, from recent studies (Pace) of mutant proteins made through site-specific mutagenesis, it appears that H bonds contribute significantly to protein folding and stability, and may make a greater contribution to stability of the native state than the hydrophobic effect. The main factor which opposes folding is chain conformational entropy.