Zobrazeno 1 - 10
of 11 925
pro vyhledávání: '"PROTEIN DYNAMICS"'
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 26, Iss , Pp 58-69 (2024)
Magnetoreception, the ability to sense magnetic fields, is widespread in animals but remains poorly understood. The leading model links this ability in migratory birds to the photo-activation of the protein cryptochrome. Magnetic information is thoug
Externí odkaz:
https://doaj.org/article/62578ac4d2ca492aa4fd6f3434b64160
Autor:
Ravdna Sarre, Olena Dobrovolska, Patrik Lundström, Diana Turcu, Tatiana Agback, Øyvind Halskau, Johan Isaksson
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-15 (2024)
Abstract Structural- and functional heterogeneity, as well as allosteric regulation, in homo-monomeric enzymes is a highly active area of research. One such enzyme is human nuclear-associated deoxyuridine 5’-triphosphate nucleotidohydrolase (dUTPas
Externí odkaz:
https://doaj.org/article/d639c9eb1b8947979994794f2b3ad784
Publikováno v:
eLife, Vol 13 (2024)
The Gram-negative bacterium Myxococcus xanthus glides on solid surfaces. Dynamic bacterial focal adhesion complexes (bFACs) convert proton motive force from the inner membrane into mechanical propulsion on the cell surface. It is unclear how the mech
Externí odkaz:
https://doaj.org/article/a402106f9c5c41c6ad2bec339a61759c
Autor:
Sarah Gersing, Thea K. Schulze, Matteo Cagiada, Amelie Stein, Frederick P. Roth, Kresten Lindorff-Larsen, Rasmus Hartmann-Petersen
Publikováno v:
Genome Biology, Vol 25, Iss 1, Pp 1-22 (2024)
Abstract Background Amino acid substitutions can perturb protein activity in multiple ways. Understanding their mechanistic basis may pinpoint how residues contribute to protein function. Here, we characterize the mechanisms underlying variant effect
Externí odkaz:
https://doaj.org/article/ae336200514940dba9340a11b8a1aaa3
Publikováno v:
Journal of Biological Engineering, Vol 18, Iss 1, Pp 1-13 (2024)
Abstract Standardized and thoroughly characterized genetic tools are a prerequisite for studying cellular processes to ensure the reusability and consistency of experimental results. The discovery of fluorescent proteins (FPs) represents a milestone
Externí odkaz:
https://doaj.org/article/80ebdd4bb1d9418093f032e9dc8df56d
Autor:
Julia Belyaeva, Matthias Elgeti
Publikováno v:
eLife, Vol 13 (2024)
Under physiological conditions, proteins continuously undergo structural fluctuations on different timescales. Some conformations are only sparsely populated, but still play a key role in protein function. Thus, meaningful structure–function framew
Externí odkaz:
https://doaj.org/article/9623c925c1fd429ca482a22af26c5386
Publikováno v:
eLife, Vol 13 (2024)
Trans-activation response (TAR) RNA-binding protein (TRBP) has emerged as a key player in the RNA interference pathway, wherein it binds to different pre-microRNAs (miRNAs) and small interfering RNAs (siRNAs), each varying in sequence and/or structur
Externí odkaz:
https://doaj.org/article/23e5b5b5201f40f3a18ae3ae6bf5087f
Autor:
Nikita V. Penkov
Publikováno v:
Frontiers in Chemistry, Vol 12 (2024)
In this work, the terahertz time-domain spectroscopy method analyzed solutions of bovine serum albumin (BSA) in two high concentrations (50 and 334 mg/mL) at three pH values (2.5, 6.5, 8.5) and the same solvents without protein, at 25°C. The spectra
Externí odkaz:
https://doaj.org/article/5b771ac22eed454190c612c1344d0eb9
Autor:
Montgomery, Julia Mae
Membrane proteins are critical to many biological processes, including molecular transport, signal transduction, and cellular interactions. Through the use of molecular dynamics (MD) simulations, we are able to model this environment at an atomistic
Externí odkaz:
https://hdl.handle.net/10919/119514
Autor:
Stephanie A Wankowicz, Ashraya Ravikumar, Shivani Sharma, Blake Riley, Akshay Raju, Daniel W Hogan, Jessica Flowers, Henry van den Bedem, Daniel A Keedy, James S Fraser
Publikováno v:
eLife, Vol 12 (2024)
In their folded state, biomolecules exchange between multiple conformational states that are crucial for their function. Traditional structural biology methods, such as X-ray crystallography and cryogenic electron microscopy (cryo-EM), produce densit
Externí odkaz:
https://doaj.org/article/df7cabe4cceb4472bbdd8fd7453b61bf