Results 291 to 300 of about 66,315 (318)

Comparison of Methodologies for Absolute Binding Free Energy Calculations of Ligands to Intrinsically Disordered Proteins. [PDF]

J Chem Theory Comput
Papadourakis M, Cournia Z, Mey ASJS, Michel J.   +3 more
europepmc   +1 more source

Toward understanding biomolecular materials comprising intrinsically disordered proteins <i>via</i> simulation and experiment.

Mol Syst Des Eng
Wang B, Zhang T, Shen S, Pochan DJ, Saven JG, Kiick KL.   +5 more
europepmc   +1 more source

Dissecting the biophysics and biology of intrinsically disordered proteins. [PDF]

Trends Biochem Sci
Banerjee PR, Holehouse AS, Kriwacki R, Robustelli P, Jiang H, Sobolevsky AI, Hurley JM, Mendell JT.   +7 more
europepmc   +1 more source

Context Dependency of Hydrophobicity in Intrinsically Disordered Proteins: Insights from a New Dewetting Free Energy-Based Hydrophobicity Scale. [PDF]

J Phys Chem B
Najafi S, Lobo S, Shell MS, Shea JE.
europepmc   +1 more source

Best practices for the manual curation of intrinsically disordered proteins in DisProt. [PDF]

Database (Oxford)
Quaglia F, Chasapi A, Nugnes MV, Aspromonte MC, Leonardi E, Piovesan D, Tosatto SCE.   +6 more
europepmc   +1 more source

Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins

Norrild RK, von Bülow S, Halldórsson E, Lindorff-Larsen K, Rogers JM, Buell AK.   +5 more
europepmc   +1 more source

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Intrinsically disordered protein

Journal of Molecular Graphics and Modelling, 2001
Proteins can exist in a trinity of structures: the ordered state, the molten globule, and the random coil. The five following examples suggest that native protein structure can correspond to any of the three states (not just the ordered state) and that protein function can arise from any of the three states and their transitions.
A K, Dunker, J D, Lawson, C J, Brown, R M, Williams, P, Romero, J S, Oh, C J, Oldfield, A M, Campen, C M, Ratliff, K W, Hipps, J, Ausio, M S, Nissen, R, Reeves, C, Kang, C R, Kissinger, R W, Bailey, M D, Griswold, W, Chiu, E C, Garner, Z, Obradovic   +19 more
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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
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Intrinsic Fluorescence of Intrinsically Disordered Proteins

2012
Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO, CIURLI, STEFANO LUCIANO
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