Results 111 to 120 of about 3,449,175 (207)
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey +4 more
wiley +1 more source
Protein Dynamics and its Correlation to Protein Activity and Stability [PDF]
The aim of this thesis is to investigate the role of fast protein dynamics (picosecond timescale) in enzyme activity and stability, and specifically to test the hypothesis that enzyme activity and stability are inversely related by their internal ...
Clement, David
core
Role of conformational dynamics in the evolution of novel enzyme function
Enzymes exist as a dynamic ensemble of conformations, each potentially playing a key role in substrate binding, the chemical transformation, or product release.
Adrian Romero-Rivera +9 more
core +1 more source
The neurokinin 1 receptor exists as full‐length (NK1L) and C‐terminally truncated (NK1S) splice variants. We show that NK1S heterodimerizes with NK1L, impairing Gαq coupling and Ca2+ mobilization while enhancing β‐arrestin1 recruitment. NK1S suppresses substance P‐driven gene expression and cell migration, revealing NK1S as an endogenous biased ...
Lan Phuong Nguyen +8 more
wiley +1 more source
Conformational Dynamics along an Enzymatic Reaction Pathway: Thymidylate Synthase, “the Movie”†
Conformational Dynamics along an Enzymatic Reaction Pathway: Thymidylate Synthase, “the Movie”†
Robert M. Stroud (30978) +1 more
core +1 more source
Human ABCE1 cannot functionally replace its yeast ortholog. Yeast–human chimera analysis identified NBD1 as a major interspecies barrier. Genetic screening yielded hABCE1 revertants that rescue yeast viability but fail to suppress aberrant translation reinitiation in the 3′ UTR.
Eriko Nakata +3 more
wiley +1 more source
MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Sho Nakajima +8 more
wiley +1 more source
Nucleic acid enzymes: The fusion of self-assembly and conformational computing
Macromolecules are the predominant physical substrate sup-porting information processing in organisms. Two key characteristics—conformational dynamics and self-assembly properties—render macro-molecules unique in this context.
Zauner, K.-P., Ramlan, E. I.
core +1 more source
Recent insights into the molecular mechanism of ubiquinol oxidation by cytochrome bc1
The review reflects on the mechanism of the catalytic reaction in cytochrome bc1: the electron bifurcation that involves the separation of two electrons derived from the quinol oxidation to opposite sides of the enzyme across the membrane. This review summarizes the long‐standing effort to understand the mechanism of quinol oxidation catalyzed by ...
Anna Wójcik‐Augustyn +2 more
wiley +1 more source
NMR RELAXATION METHODS TO DETECT PROTEIN DYNAMICS: EVALUATION OF ACCURACY, IMPROVEMENT OF THE METHODOLOGY, AND ITS APPLICATION [PDF]
Proteins are dynamic molecules whose ability to undergo conformational changes and fluctuations can impact their biological function, such as enzyme catalysis and substrate recognition. Mutations or perturbations that do not significantly change protein
Myint, Wazo
core

