Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Marcus B. Kubitzki"'
Publikováno v:
PLoS Computational Biology, Vol 6, Iss 5, p e1000774 (2010)
We present molecular dynamics simulations of unliganded human hemoglobin (Hb) A under physiological conditions, starting from the R, R2, and T state. The simulations were carried out with protonated and deprotonated HC3 histidines His(beta)146, and t
Externí odkaz:
https://doaj.org/article/141ab86c8c8a46aea94aa2dc50f91b07
Publikováno v:
From Protein Structure to Function with Bioinformatics ISBN: 9789402410679
From Protein Structure to Function with Bioinformatics ISBN: 9781402090578
From Protein Structure to Function with Bioinformatics
From protein structure to function with bioinformatics
From Protein Structure to Function with Bioinformatics ISBN: 9781402090578
From Protein Structure to Function with Bioinformatics
From protein structure to function with bioinformatics
Understanding protein function requires detailed knowledge about protein dynamics , i.e. the different conformational states the system can adopt. Despite substantial experimental progress, simulation techniques such as molecular dynamics (MD) curren
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8af07340003b73bbd987abafa6217625
https://doi.org/10.1007/978-94-024-1069-3_12
https://doi.org/10.1007/978-94-024-1069-3_12
Autor:
Bert L. de Groot, Marcus B. Kubitzki
Publikováno v:
Structure
SummaryWe report on an atomistic molecular dynamics simulation of the complete conformational transition of Escherichia coli adenylate kinase (ADK) using the recently developed TEE-REX algorithm. Two phases characterize the transition pathway of ADK,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::605d154ac50943bc6c261ec71620c426
https://hdl.handle.net/11858/00-001M-0000-0012-DB11-411858/00-001M-0000-0012-DB12-2
https://hdl.handle.net/11858/00-001M-0000-0012-DB11-411858/00-001M-0000-0012-DB12-2
Autor:
Marcus B. Kubitzki, Bert L. de Groot
Publikováno v:
Biophysical Journal. (12):4262-4270
Today's standard molecular dynamics simulations of moderately sized biomolecular systems at full atomic resolution are typically limited to the nanosecond timescale and therefore suffer from limited conformational sampling. Efficient ensemble-preserv