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Wyszukujesz frazę "Gonzalez, Miguel" wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
VIBES: Visionary Ingenuity Boosting European Spacecraft. Managing microvibrations for the future of spaceflight
Autorzy:
Garcia, Antonio
Gust, Tim
Basata, Enes
Gersting, Tim
Deka, Michal
Thiele, Sven
Salah, Mohammad
Koerner, Matias Bestard
Runte, Torben
Gonzalez, Miguel
Powiązania:
https://bibliotekanauki.pl/articles/27309883.pdf
Data publikacji:
2023
Wydawca:
Polska Akademia Nauk. Czasopisma i Monografie PAN
Tematy:
microvibrations
isolation
satellite architectures
metrology
control
mikrowibracje
izolacja
metrologia
kontrola
Opis:
Microvibrations are mechanical oscillations caused by components such as the reaction wheels of an attitude control system of a spacecraft. These microvibrations are transferred through the spacecraft structure onto important instruments (e.g., optical instruments), causing those to produce diminished results (e.g., reduced image quality, imprecise geolocation etc.). At the present state, microvibrations in spacecraft cannot be actively controlled because their very high frequencies of up to 1000 Hz are above the control bandwidth a current attitude control system can provide. However, being able to reduce the effects of microvibrations on a space mission is becoming increasingly more critical as the envelope of future optical satellite missions expands. Furthermore, the advancements made in the performance of small satellites as well as the growing interest in laser and quantum communication call for a cost-efficient solution for managing microvibrations. This paper describes how cheap MEMS-based measurement systems have already proven that they are a potential solution. Showing high sensitivity and low-noise performance while allowing fast and easy prototyping.
Źródło:
Archive of Mechanical Engineering; 2023, LXX, 2; 183--197
0004-0738
Pojawia się w:
Archive of Mechanical Engineering
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Computational model of abiogenic amino acid condensation to obtain a polar amino acid profile
Autorzy:
Polanco, Carlos
Buhse, Thomas
Samaniego, José
Castañón González, Jorge
Estrada, Miguel
Powiązania:
https://bibliotekanauki.pl/articles/1039283.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
amino acids
proteinoids
origins of life
polarity
computer simulations
Opis:
In accordance with the second law of thermodynamics, the Universe as a whole tends to higher entropy. However, the sequence of far-from-equilibrium events that led to the emergence of life on Earth could have imposed order and complexity during the course of chemical reactions in the so-called primordial soup of life. Hence, we may expect to find characteristic profiles or biases in the prebiotic product mixtures, as for instance among the first amino acids. Seeking to shed light on this hypothesis, we have designed a high performance computer program that simulates the spontaneous formation of the amino acid monomers in closed environments. The program was designed in reference to a prebiotic scenario proposed by Sydney W. Fox. The amino acid abundances and their polarities as the two principal biases were also taken into consideration. We regarded the computational model as exhaustive since 200 000 amino acid dimers were formed by simulation, subsequently expressed in a vector and compared with the corresponding amino acid dimers that were experimentally obtained by Fox. We found a very high similarity between the experimental results and our simulations.
Źródło:
Acta Biochimica Polonica; 2014, 61, 2; 253-258
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Identification of proteins associated with amyloidosis by polarity index method
Autorzy:
Polanco, Carlos
Samaniego, José
Uversky, Vladimir
Castañón-González, Jorge
Buhse, Thomas
Leopold-Sordo, Marili
Madero-Arteaga, Alejandro
Morales-Reyes, Alicia
Tavera-Sierra, Lourdes
González-Bernal, Jesus
Arias-Estrada, Miguel
Powiązania:
https://bibliotekanauki.pl/articles/1039130.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Polarity index method
natively unfolded proteins
intrinsically disordered proteins
natively folded proteins
neurons
amyloidosis
amyloid
amyloidogenic protein
Opis:
There is a natural protein form, insoluble and resistant to proteolysis, adopted by many proteins independently of their amino acid sequences via specific misfolding-aggregation process. This dynamic process occurs in parallel with or as an alternative to physiologic folding, generating toxic protein aggregates that are deposited and accumulated in various organs and tissues. These proteinaceous deposits typically represent bundles of β-sheet-enriched fibrillar species known as the amyloid fibrils that are responsible for serious pathological conditions, including but not limited to neurodegenerative diseases, grouped under the term amyloidoses. The proteins that might adopt this fibrillar conformation are some globular proteins and natively unfolded (or intrinsically disordered) proteins. Our work shows that intrinsically disordered and intrinsically ordered proteins can be reliably identified, discriminated, and differentiated by analyzing their polarity profiles generated using a computational tool known as the polarity index method (Polanco & Samaniego, 2009; Polanco et al., 2012; 2013; 2013a; 2014; 2014a; 2014b; 2014c; 2014d). We also show that proteins expressed in neurons can be differentiated from proteins in these two groups based on their polarity profiles, and also that this computational tool can be used to identify proteins associated with amyloidoses. The efficiency of the proposed method is high (i.e. 70%) as evidenced by the analysis of peptides and proteins in the APD2 database (2012), AVPpred database (2013), and CPPsite database (2013), the set of selective antibacterial peptides from del Rio et al. (2001), the sets of natively unfolded and natively folded proteins from Oldfield et al. (2005), the set of human revised proteins expressed in neurons, and non-human revised proteins expressed in neurons, from the Uniprot database (2014), and also the set of amyloidogenic proteins from the AmyPDB database (2014).
Źródło:
Acta Biochimica Polonica; 2015, 62, 1; 41-55
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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