Results 111 to 120 of about 32,287 (136)

Searching and Using MobiDB Resource 6 to Explore Predictions and Annotations for Intrinsically Disordered Proteins. [PDF]

Curr Protoc
Aspromonte MC, Quaglia F, Monzon AM, Clementel D, Del Conte A, Piovesan D, Tosatto SCE.   +6 more
europepmc   +1 more source

Size, Conformation, and Local Domains of Single-Chain Nanoparticles with Intrachain Covalent, Dipolar, and Electrostatic Interactions: Toward Artificial Intrinsically Disordered Proteins. [PDF]

Macromolecules
Iguaran M, Gutierrez-Lkourt S, Verde-Sesto E, Maestro A, Pomposo JA.   +4 more
europepmc   +1 more source

IDP-Bert: Predicting Properties of Intrinsically Disordered Proteins Using Large Language Models. [PDF]

J Phys Chem B
Mollaei P, Sadasivam D, Guntuboina C, Barati Farimani A.   +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

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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Intrinsic disorder in S100 proteins

Molecular BioSystems, 2011
Although the members of the largest subfamily of the EF-hand proteins, S100 proteins, are evolutionarily young, their functional diversity is extremely broad, partly due to their ability to adapt to various targets. This feature is a hallmark of intrinsically disordered proteins (IDPs), but none of the S100 proteins are recognized as IDPs.
Sergei E, Permyakov, Ramis G, Ismailov, Bin, Xue, Alexander I, Denesyuk, Vladimir N, Uversky, Eugene A, Permyakov   +5 more
openaire   +3 more sources

Frustration-induced protein intrinsic disorder

The Journal of Chemical Physics, 2013
Spontaneous folding into a specific native structure is the most important property of protein to perform their biological functions within organisms. Spontaneous folding is understood on the basis of an energy landscape picture based on the minimum frustration principle.
Katsuyoshi, Matsushita, Macoto, Kikuchi
openaire   +2 more sources