Results 71 to 80 of about 38,411 (253)
Optimizing enzyme thermostability by combining multiple mutations using protein language model
mLifeOptimizing enzyme thermostability is essential for advancements in protein science and industrial applications. Currently, (semi‐)rational design and random mutagenesis methods can accurately identify single‐point mutations that enhance enzyme ...
Jiahao Bian +4 more
doaj +1 more source
The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties
Frontiers in Bioengineering and Biotechnology, 2017 Lipases are important industrial enzymes. Most of the lipases operate at lipid–water interfaces enabled by a mobile lid domain located over the active site. Lid protects the active site and hence responsible for catalytic activity. In pure aqueous media,
Faez Iqbal Khan +6 more
doaj +1 more source
Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins. [PDF]
Protein SciAbstract De novo protein design often produces thermostable proteins that denature above 100°C, which complicates the analysis of their stability. Thermostable proteins can be unfolded by combined chemical and thermal denaturation followed by global analysis of multiple melting curves.
Lampinen V +7 more
europepmc +2 more sources
Advanced Science, EarlyView.In the post‐stroke brain, Foxa2 induces the transcriptional upregulation of Nrsn1 in NSCs. Nrsn1 functionally couples with Smarcc1, modulating its nuclear availability and protein abundance, thereby influencing Smarcc1‐associated regulatory programs linked to neuronal lineage commitment. Through this coupling, Nrsn1 promotes the differentiation of NSCs
Ruolin Zhang +18 more
wiley +1 more source
In Vitro Selection of Functional Neoproteins Containing Highly Fluorinated Cores
Angewandte Chemie, EarlyView.The generation of neoproteins—functional proteins containing unnatural amino acids—is a key goal in synthetic biology. We develop a platform to discover neoproteins with specified bioactivity from trillion‐member sequence libraries, using genetic code reprogramming, in vitro selection and microwave peptide synthesis.
Adam Beattie +5 more
wiley +2 more sources
Thermostability of Ap-contained oligo-microsphere.
, 2016 Thermostability of Ap-contained oligo-microsphere.
Ok Chan Jeong (2101423) +5 more
core +1 more source
Endoglucanases: insights into thermostability for biofuel applications [PDF]
, 2013 Obtaining bioethanol from cellulosic biomass involves numerous steps, among which the enzymatic conversion of the polymer to individual sugar units has been a main focus of the biotechnology industry.
Yennamalli, Ragothaman M. +9 more
core +1 more source
Engineered Transformer Base Editor with Enhanced Editing Efficiency
Advanced Science, EarlyView.A highly efficient transformer base editor system achieves robust genomic editing in a humanized mouse model. This work establishes a versatile and translatable platform, opening new avenues for precision gene therapy. ABSTRACT Canonical cytosine base editors (CBEs) achieve precise C‐to‐T conversions without inducing DNA double‐strand breaks (DSBs ...
Bowen Chen +5 more
wiley +1 more source
Angewandte Chemie, EarlyView.A biobased tricyclic thionolactone undergoes selective isomerization ring‐opening polymerization to yield a high‐molecular‐weight polythioester with an exceptionally high Tg of 171°C, exceeding that of the analogous polyester. The polythioester efficiently depolymerizes through backbiting, while its hydrolysis and methanolysis reveal the critical ...
Eva Harsevoort +4 more
wiley +2 more sources
Protein thermostability in extremophiles
, 1998 Thermostability of a protein is a property which cannot be attributed to the presence of a particular amino acid or to a post synthetic modification. Thermostability seems to be a property acquired by a protein through many small structural modifications
Paul C. Engel +8 more
core +1 more source