Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Sashary Ramos"'
Autor:
Célia Millon, Johannes Schmidt, Sashary Ramos, Eliane P. van Dam, Adrian Buchmann, Clara Saraceno, Fabio Novelli
Publikováno v:
AIP Advances, Vol 12, Iss 11, Pp 115319-115319-5 (2022)
Liquid water is one of the most studied substances, yet many of its properties are difficult to rationalize. The uniqueness of water is rooted in the dynamic network of hydrogen-bonded molecules with relaxation time constants of about one picosecond.
Externí odkaz:
https://doaj.org/article/5942f89a644c4c8eba9530f8cbb7b4fe
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
The importance of conformational dynamics to protein function is now well-appreciated. An outstanding question is whether they are involved in the effector role played by putidaredoxin (Pdx) in its reduction of the O2 complex of cytochrome P450cam (P
Externí odkaz:
https://doaj.org/article/0a6529b4f9b545629f389ce1dbcf3340
Autor:
Eliane P. van Dam, Benedikt König, Sashary Ramos, Ellen M. Adams, Gerhard Schwaab, Martina Havenith
Publikováno v:
Physical chemistry chemical physics : PCCP. 24(45)
Aqueous hyaluronan solutions form an elastic hydrogel within a narrow pH range, around pH 2.4, making this a model system to study the conformational changes of the hydrogen bond network upon gelation. This pH-dependent behavior allows us to probe wa
Publikováno v:
Biochemistry
Cytochrome P450s are diverse and powerful catalysts that can activate molecular oxygen to oxidize a wide variety of substrates. Catalysis relies on effective uptake of two electrons and two protons. For cytochrome P450cam, an archetypal member of the
Publikováno v:
Biophys J
Structural heterogeneity and the dynamics of the complexes of enzymes with substrates can determine the selectivity of catalysis; however, fully characterizing how remains challenging as heterogeneity and dynamics can vary at the spatial level of an
Autor:
Simone Pezzotti, Federico Sebastiani, Eliane P. van Dam, Sashary Ramos, Valeria Conti Nibali, Gerhard Schwaab, Martina Havenith
Hydration free energies are dictated by a subtle balance of hydrophobic and hydrophilic interactions. which is crucial for many biological processes and technological applications, such as protein folding and molecular recognition. Whereas so far the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ff66e5bb0caaab0dbbefd7eca4103ce
https://doi.org/10.26434/chemrxiv-2022-7wkv6
https://doi.org/10.26434/chemrxiv-2022-7wkv6
Autor:
Simone Pezzotti, Federico Sebastiani, Eliane P. van Dam, Sashary Ramos, Valeria Conti Nibali, Gerhard Schwaab, Martina Havenith
Publikováno v:
Angewandte Chemie International Edition
Hydration free energies are dictated by a subtle balance of hydrophobic and hydrophilic interactions. We present here a spectroscopic approach, which gives direct access to the two main contributions: Using THz-spectroscopy to probe the frequency ran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1f3520c813831f4670421f7daf67b06
https://hdl.handle.net/11570/3230119
https://hdl.handle.net/11570/3230119
Publikováno v:
Proceedings of the 2021 International Symposium on Molecular Spectroscopy.
Publikováno v:
Physical Chemistry Chemical Physics. 21:780-788
The conformational heterogeneity and dynamics of protein side chains contribute to function, but investigating exactly how is hindered by experimental challenges arising from the fast timescales involved and the spatial heterogeneity of protein struc
Publikováno v:
Proceedings of the 2020 International Symposium on Molecular Spectroscopy.