نتایج جستجو برای: thermophilic proteins

تعداد نتایج: 561306  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Arnon Paz David Mester Ivan Baca Eviatar Nevo Abraham Korol

The mechanism of an organism's adaptation to high temperatures has been investigated intensively in recent years. It was suggested that the macromolecules of thermophilic microorganisms (especially proteins) have structural features that enhance their thermostability. We compared mRNA sequences of 72 fully sequenced prokaryotic proteomes (14 thermophilic and 58 mesophilic species). Although the...

Journal: :The Journal of chemical physics 2014
Bartosz Różycki Marek Cieplak

We study four citrate synthase homodimeric proteins within a structure-based coarse-grained model. Two of these proteins come from thermophilic bacteria, one from a cryophilic bacterium and one from a mesophilic organism; three are in the closed and two in the open conformations. Even though the proteins belong to the same fold, the model distinguishes the properties of these proteins in a way ...

2013
Christopher J. Reed Hunter Lewis Eric Trejo Vern Winston Caryn Evilia

Extremophiles, especially those in Archaea, have a myriad of adaptations that keep their cellular proteins stable and active under the extreme conditions in which they live. Rather than having one basic set of adaptations that works for all environments, Archaea have evolved separate protein features that are customized for each environment. We categorized the Archaea into three general groups ...

2018
Elrike Frenzel Jelmer Legebeke Atze van Stralen Richard van Kranenburg Oscar P. Kuipers

Background Fluorescent reporter proteins (FP) have become an indispensable tool for the optimization of microbial cell factories and in synthetic biology per se. The applicability of the currently available FPs is, however, constrained by species-dependent performance and misfolding at elevated temperatures. To obtain functional reporters for thermophilic, biotechnologically important bacteria ...

Journal: :Methods in enzymology 2001
S W Englander R Hiller

The naturally occurring hydrogen exchange of protein molecules can provide nonperturbing site-resolved measurements of protein stability and flexibility and changes therein. The measurement and understanding of these issues is especially pertinent to studies of thermophilic proteins. This chapter briefly reviews the considerations necessary for measuring hydrogen exchange and translating HX mea...

Journal: :Bioresources and Bioprocessing 2021

Abstract Thermophilic Argonaute proteins (Agos) have been shown to utilize small DNA guides for cleaving complementary in vitro, which shows great potential nucleic acid detection. In this study, we explored mesophilic Agos the detection of molecule by cooperating with allosteric transcription factors (aTFs). Two from bacteria, Paenibacillus borealis ( Pb Ago) and Brevibacillus laterosporus Bl ...

2007
Stefan L. Ameres Dmitry Shcherbakov Ekaterina Nikonova Wolfgang Piendl Renée Schroeder Katharina Semrad

RNA chaperone activity is defined as the ability of proteins to either prevent RNA from misfolding or to open up misfolded RNA conformations. One-third of all large ribosomal subunit proteins from E. coli display this activity, with L1 exhibiting one of the highest activities. Here, we demonstrate via the use of in vitro trans- and cis-splicing assays that the RNA chaperone activity of L1 is co...

Journal: :Proteins 2012
Yunqi Li Jian Zhang David Tai C Russell Middaugh Yang Zhang Jianwen Fang

Designing proteins with enhanced thermo-stability has been a main focus of protein engineering because of its theoretical and practical significance. Despite extensive studies in the past years, a general strategy for stabilizing proteins still remains elusive. Thus effective and robust computational algorithms for designing thermo-stable proteins are in critical demand. Here we report PROTS, a...

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