- ORCID iD
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0000-0003-4718-4911
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Protein dynamics and conformational heterogeneity in solution are not well captured by AlphaFold and other computational approaches
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Investigating protein flexibility using molecular dynamics simulations of α-1 acid glycoprotein and large-scale normal mode analysis of AlphaFold models
(2025) -
- Journal Article
- A1
- open access
Gradations in protein dynamics captured by experimental NMR are not well represented by AlphaFold2 models and other computational metrics
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Supplementary data frames, AlphaFold models, Normal Mode Analysis (NMA) Data, and NMA of Corresponding NMR Ensembles in the S2RCI, MD, and S2 Datasets for "Gradations in protein dynamics captured by experimental NMR are not well represented by AlphaFold2 models and other computational metrics"
(2024) -
- Journal Article
- A1
- open access
Conformational dynamics of α‐1 acid glycoprotein (AGP) in cancer : a comparative study of glycosylated and unglycosylated AGP
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- Journal Article
- A1
- open access
Challenges in describing the conformation and dynamics of proteins with ambiguous behavior
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- Conference Paper
- C3
- open access
Dissecting conformational dynamics of α-1 acid glycoprotein (AGP) : a study of glycosylated and un-glycosylated mutants
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Dissecting the conformational dynamics of α-1 acid glycoprotein (AGP) in cancer : a comparative study of glycosylated and un glycosylated AGP mutants
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- Conference Paper
- C3
- open access
Dissecting the conformational dynamics of α-1 acid glycoprotein (AGP) in cancer : a comparative study of glycosylated and un glycosylated AGP mutants
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- Conference Paper
- C3
- open access
Backbone dynamics alignment of proteins : harnessing biophysical fingerprints in pairwise sequence alignment