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Biochemistry (Moscow), 2010
Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state
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Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state
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Replica-exchange molecular dynamics method for protein folding
, 1999Y. Sugita, Y. Okamoto
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Molecular chaperones in cellular protein folding
Nature, 1996F. Hartl
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Heterogeneity in Protein Folding and Unfolding Reactions
Chemical Reviews, 2022Sandhya Bhatia, Jayant B Udgaonkar
exaly
Microphase Separation‐Driven Sequential Self‐Folding of Nanocomposite Hydrogel/Elastomer Actuators
Advanced Functional Materials, 2022Jinhye Bae
exaly
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
Nature, 1999H. Harding, Yuhong Zhang, D. Ron
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The impact of the endoplasmic reticulum protein-folding environment on cancer development
Nature Reviews. Cancer, 2014Miao Wang, R. Kaufman
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