Exploring nucleation pathways in distinct physicochemical environments unveiling novel options to modulate and optimize protein crystallization (2022)
- Authors:
- Autor USP: BARRA, ANGÉLICA LUANA CARRILLO - IFSC
- Unidade: IFSC
- DOI: 10.3390/cryst12030437
- Subjects: NUCLEAÇÃO; CRISTALIZAÇÃO
- Keywords: Phase transition; Multiple nucleation pathways; Mesoscopic ordered clusters; Pulsed electric field; Dynamic light scattering; Depolarized dynamic light scattering
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
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- Cor do Acesso Aberto: gold
- Licença: cc-by
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ABNT
WANG, Mengying et al. Exploring nucleation pathways in distinct physicochemical environments unveiling novel options to modulate and optimize protein crystallization. Crystals, v. 12, n. 3, p. 437-1-437-22, 2022Tradução . . Disponível em: https://doi.org/10.3390/cryst12030437. Acesso em: 16 maio 2024. -
APA
Wang, M., Barra, A. L. C., Brognaro, H., & Betzel, C. (2022). Exploring nucleation pathways in distinct physicochemical environments unveiling novel options to modulate and optimize protein crystallization. Crystals, 12( 3), 437-1-437-22. doi:10.3390/cryst12030437 -
NLM
Wang M, Barra ALC, Brognaro H, Betzel C. Exploring nucleation pathways in distinct physicochemical environments unveiling novel options to modulate and optimize protein crystallization [Internet]. Crystals. 2022 ; 12( 3): 437-1-437-22.[citado 2024 maio 16 ] Available from: https://doi.org/10.3390/cryst12030437 -
Vancouver
Wang M, Barra ALC, Brognaro H, Betzel C. Exploring nucleation pathways in distinct physicochemical environments unveiling novel options to modulate and optimize protein crystallization [Internet]. Crystals. 2022 ; 12( 3): 437-1-437-22.[citado 2024 maio 16 ] Available from: https://doi.org/10.3390/cryst12030437 - Structure, function, and dynamics of vitamin B6 biosynthesis enzymes from Staphylococcus aureus
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Informações sobre o DOI: 10.3390/cryst12030437 (Fonte: oaDOI API)
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