Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Heiko Lammert"'
Autor:
Susmita Roy, Heiko Lammert, Ryan L Hayes, Bin Chen, Regan LeBlanc, T Kwaku Dayie, José N Onuchic, Karissa Y Sanbonmatsu
Publikováno v:
PLoS Computational Biology, Vol 13, Iss 3, p e1005406 (2017)
Our 13C- and 1H-chemical exchange saturation transfer (CEST) experiments previously revealed a dynamic exchange between partially closed and open conformations of the SAM-II riboswitch in the absence of ligand. Here, all-atom structure-based molecula
Externí odkaz:
https://doaj.org/article/8ab6a05fea3742f2b2caaf5cc33b1883
Autor:
Jeffrey K Noel, Mariana Levi, Mohit Raghunathan, Heiko Lammert, Ryan L Hayes, José N Onuchic, Paul C Whitford
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 3, p e1004794 (2016)
Molecular dynamics simulations with coarse-grained or simplified Hamiltonians have proven to be an effective means of capturing the functionally important long-time and large-length scale motions of proteins and RNAs. Originally developed in the cont
Externí odkaz:
https://doaj.org/article/011d0a54cc4545b18638869668dd3097
Autor:
Ellinor Haglund, Joanna I Sulkowska, Jeffrey K Noel, Heiko Lammert, José N Onuchic, Patricia A Jennings
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 6, p e1003613 (2014)
A four-helix bundle is a well-characterized motif often used as a target for designed pharmaceutical therapeutics and nutritional supplements. Recently, we discovered a new structural complexity within this motif created by a disulphide bridge in the
Externí odkaz:
https://doaj.org/article/0b1317bdbf2b483687a4e26c0b16044b
Publikováno v:
PLoS Computational Biology, Vol 8, Iss 11, p e1002776 (2012)
Energetic frustration in protein folding is minimized by evolution to create a smooth and robust energy landscape. As a result the geometry of the native structure provides key constraints that shape protein folding mechanisms. Chain connectivity in
Externí odkaz:
https://doaj.org/article/18c8c2077594479c9fbf312dc2850f09
Publikováno v:
The Journal of Physical Chemistry B. 123:1505-1511
We develop a simple, coarse-grained approach for simulating the folding of the Beet Western Yellow Virus (BWYV) pseudoknot toward the goal of creating a transferable model that can be used to study other small RNA molecules. This approach combines a
Publikováno v:
Journal of the American Chemical Society. 140:1203-1206
The rational design of genetically encoded fluorescent biosensors, which can detect rearrangements of target proteins via interdomain allostery, is hindered by the absence of mechanistic understanding of the underlying photophysics. Here, we focus on
Publikováno v:
Nucleic Acids Research
Investigations of most riboswitches remain confined to the ligand-binding aptamer domain. However, during the riboswitch mediated transcription regulation process, the aptamer domain and the expression platform compete for a shared strand. If the exp
Publikováno v:
The journal of physical chemistry. B. 122(49)
We unravel the internal and collective modes of a widely studied 58-nucleotide rRNA fragment in solvent using atomically detailed molecular dynamics simulations. The variation of lifetimes for water hydrogen bonds with nucleotide groups indicates het
Autor:
Lannie Nguyen, Ellinor Haglund, Nicholas P. Schafer, José N. Onuchic, Heiko Lammert, Patricia A. Jennings
Publikováno v:
The Journal of biological chemistry, vol 293, iss 33
The pleiotropic hormone leptin has a pivotal role in regulating energy balance by inhibiting hunger and increasing energy expenditure. Homozygous mutations found in the leptin gene are associated with extreme obesity, marked hyperphagia, and impaired
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d30ffadc7096087d8f0f06dba565f313
https://escholarship.org/uc/item/974784sc
https://escholarship.org/uc/item/974784sc
Autor:
Rachel Nechushtai, Amy Liu, José N. Onuchic, Yang Sung Sohn, Merav Darash-Yahana, Ron Mittler, Colin H. Lipper, Luhua Song, Patricia A. Jennings, Heiko Lammert, Ola Karmi
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 115, iss 2
The NEET family is a relatively new class of three related [2Fe-2S] proteins (CISD1–3), important in human health and disease. While there has been growing interest in the homodimeric gene products of CISD1 (mitoNEET) and CISD2 (NAF-1), the importa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93876ba25546c331a02e25a76ed9d1af
https://europepmc.org/articles/PMC5777063/
https://europepmc.org/articles/PMC5777063/