Results 111 to 120 of about 27,570 (293)

The Lrs14‐Like AbfR1 Homolog From Metallosphaera sedula Is a Nucleoid‐Organizing Protein

MicrobiologyOpen, Volume 14, Issue 5, October 2025.
Nucleoid organization in Crenarchaeota involves diverse small DNA‐binding proteins. The Lrs14‐type protein AbfR1 from Metallosphaera sedula binds nonsequence specifically across the genome and induces DNA condensation. These findings suggest a structural role for AbfR1Ms in chromatin architecture, functionally resembling bacterial nucleoid‐associated ...
Veerke De Kock, Ronnie Willaert, Yannick Gansemans, Filip Van Nieuwerburgh, Rani Baes, Eveline Peeters   +5 more
wiley   +1 more source

Comparative Genome Analysis of Bacillus sporothermodurans with Its Closest Phylogenetic Neighbor, Bacillus oleronius, and Bacillus cereus and Bacillus subtilis Groups

Microorganisms, 2020
Bacillus sporothermodurans currently possesses one of the most highly heat-resistant spores (HRS), which can withstand ultra-high temperature (UHT) processing. Determination of multiple whole genome sequences of B.
Rodney Owusu-Darko, Mushal Allam, Arshad Ismail, Carlos A. S. Ferreira, Sílvia D. de Oliveira, Elna M. Buys   +5 more
doaj   +1 more source

Dose, exposure time, and resolution in Serial X-ray Crystallography

, 2007
The resolution of X-ray diffraction microscopy is limited by the maximum dose that can be delivered prior to sample damage. In the proposed Serial Crystallography method, the damage problem is addressed by distributing the total dose over many identical ...
Chapman, H. N., Doak, R. B., Fromme, P., Hembree, G., Howells, M., Rez, P., Schmidt, K., Shapiro, D., Spence, J. C. H., Starodub, D., Weierstall, U.   +10 more
core   +1 more source

Rubisco Assembly in the Chloroplast

Frontiers in Molecular Biosciences, 2018
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source.
Anna Vitlin Gruber, Leila Feiz
doaj   +1 more source

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

Cell, 1995
The chaperonin GroEL is a large, double-ring structure that, together with ATP and the cochaperonin GroES, assists protein folding in vivo. GroES forms an asymmetric complex with GroEL in which a single GroES ring binds one end of the GroEL cylinder ...
Jonathan S. Weissman, Jonathan S. Weissman, Corinne M. Hohl, Corinne M. Hohl, O. Kovalenko, Y. Kashi, Shaoxia Chen, K. Braig, H. Saibil, W. Fenton, Arthur L. Norwich, Arthur L. Norwich   +11 more
semanticscholar   +1 more source

Screening of molecular elements and improvement of heat resistance in a thermophilic bacterium

Engineering Microbiology
Engineering microorganisms to withstand extreme temperatures (>80 °C) remains a critical challenge in industrial biotechnology owing to limited genetic tools and poor mechanistic understanding of microbial thermoadaptation.
Jie Cui, Caifeng Li, Gongze Cao, Yuxia Wu, Shouying Xu, Youming Zhang, Xiaoying Bian, Qiang Tu, Wentao Zheng   +8 more
doaj   +1 more source

The Poet\u27s Corner [PDF]

, 1986
A collection of poems sent in by ...

core   +1 more source

Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations. [PDF]

, 2011
Protein stability is widely recognized as a major evolutionary constraint. However, the relation between mutation-induced perturbations of protein stability and biological fitness has remained elusive.
Eugene Shakhnovich, Shimon Bershtein
core   +1 more source

Dynamic complexes in the chaperonin-mediated protein folding cycle

Frontiers in Molecular Biosciences, 2016
The GroEL-GroES chaperonin system is probably one of the most studied chaperone systems at the level of the molecular mechanism. Since the first reports of a bacterial gene involved in phage morphogenesis in 1972, these proteins have stimulated ...
Celeste Weiss, Fady Jebara, Shahar Nisemblat, Abdussalam Azem   +3 more
doaj   +1 more source

In silico engineering of aggregation-prone recombinant proteins for substrate recognition by the chaperonin GroEL

BMC Genomics, 2012
Background Molecular chaperones appear to have been evolved to facilitate protein folding in the cell through entrapment of folding intermediates on the interior of a large cavity formed between GroEL and its co-chaperonin GroES.
Kumar Vipul, Punetha Ankita, Sundar Durai, Chaudhuri Tapan K   +3 more
doaj   +1 more source