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Fuzzy Logic is a good model for the human ability to compute words. It is based on the theory of fuzzy set. A fuzzy set is different from a classical set because it breaks the Law of the Excluded Middle. In fact, an item may belong to a fuzzy set and its complement at the same time and with the same or different degree of membership. The degree of membership of an item in a fuzzy set can be any real number included between 0 and 1. This property enables us to deal with all those statements of which truths are a matter of degree. Fuzzy logic plays a relevant role in the field of Artificial Intelligence because it enables decision-making in complex situations, where there are many intertwined variables involved. Traditionally, fuzzy logic is implemented through software on a computer or, even better, through analog electronic circuits. Recently, the idea of using molecules and chemical reactions to process fuzzy logic has been promoted. In fact, the molecular word is fuzzy in its essence. The overlapping of quantum states, on the one hand, and the conformational heterogeneity of large molecules, on the other, enable context-specific functions to emerge in response to changing environmental conditions. Moreover, analog input–output relationships, involving not only electrical but also other physical and chemical variables can be exploited to build fuzzy logic systems. The development of “fuzzy chemical systems” is tracing a new path in the field of artificial intelligence. This new path shows that artificially intelligent systems can be implemented not only through software and electronic circuits but also through solutions of properly chosen chemical compounds. The design of chemical artificial intelligent systems and chemical robots promises to have a significant impact on science, medicine, economy, security, and wellbeing. Therefore, it is my great pleasure to announce a Special Issue of Molecules entitled “The Fuzziness in Molecular, Supramolecular, and Systems Chemistry.” All researchers who experience the Fuzziness of the molecular world or use Fuzzy logic to understand Chemical Complex Systems will be interested in this book.

Research & information: general --- Biology, life sciences --- fuzzy logic --- complexity --- chemical artificial intelligence --- human nervous system --- fuzzy proteins --- conformations --- photochromic compounds --- qubit --- protein dynamics --- conformational heterogeneity --- promiscuity --- fuzzy complexes --- higher-order structures --- protein evolution --- fuzzy set theory --- artificial intelligence --- GCN4 mimetic --- peptides–DNA --- E:Z photoisomerization --- conformational fuzziness --- photoelectrochemistry --- wide bandgap semiconductor --- artificial neuron --- in materio computing --- neuromorphic computing --- intrinsically disordered protein --- intrinsically disordered protein region --- liquid–liquid phase transition --- protein–protein interaction --- protein–nucleic acid interaction --- proteinaceous membrane-less organelle --- fuzzy complex. --- d-TST --- activation energy --- Transitivity plot --- solution kinetic --- Maxwell–Boltzmann path --- Euler’s formula for the exponential --- activation --- transitivity --- transport phenomena --- moonlighting proteins --- intrinsically disordered proteins --- metamorphic proteins --- morpheeins --- n/a --- peptides-DNA --- liquid-liquid phase transition --- protein-protein interaction --- protein-nucleic acid interaction --- Maxwell-Boltzmann path --- Euler's formula for the exponential

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Disordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999. First, it was generally thought for more than a decade that disordered proteins or disordered parts of proteins have different amino acid compositions than folded proteins, and various prediction methods were developed based on this principle. These methods were suitable for distinguishing between the disordered (unstructured) and structured proteins known at that time. In addition, they could predict the site where a folded protein binds to the disordered part of a protein, shaping the latter into a well-defined 3D structure. Recently, however, evidence has emerged for a new type of disordered protein family whose members can undergo coupled folding and binding without the involvement of any folded proteins. Instead, they interact with each other, stabilizing their structure via “mutual synergistic folding” and, surprisingly, they exhibit the same residue composition as the folded protein. Increasingly more examples have been found where disordered proteins interact with non-protein macromolecules, adding to the already large variety of protein–protein interactions. There is also a very new phenomenon when proteins are involved in phase separation, which can represent a weak but functionally important macromolecular interaction. These phenomena are presented and discussed in the chapters of this book.

Research & information: general --- Biology, life sciences --- intrinsically disordered proteins --- epiproteome --- disordered protein platform --- molecular recognition feature --- post-translational modifications --- physiological homeostasis --- stress response --- RIN4 --- p53 --- molecular machines --- intrinsically disordered protein --- membrane-less organelle --- neurodegenerative disease --- p300 HAT acetylation --- post-translational modification --- protein aggregation --- Tau fibrillation --- intrinsically disorder proteins --- disorder-to-order regions --- protein–RNA interactions --- unstructured proteins --- conformational plasticity --- disordered protein --- folding --- ribosomal protein --- spectroscopy --- protein stability --- temperature response --- protein thermostability --- salt bridges --- meta strategy --- dual threshold --- significance voting --- decision tree based artificial neural network --- protein intrinsic disorder --- intrinsic disorder --- intrinsic disorder prediction --- intrinsically disordered region --- protein conformation --- transcriptome --- RNA sequencing --- Microarray --- differentially regulated genes --- gene ontology analysis --- functional analysis --- intrinsically disordered --- structural disorder --- correlated mutations --- co-evolution --- evolutionary couplings --- residue co-variation --- interaction surface --- residue contact network --- dehydron --- homodimer --- hydrogen bond --- inter-subunit interaction --- ion pair --- mutual synergistic folding --- solvent-accessible surface area --- stabilization center --- MLL proteins --- MLL4 --- lncRNA --- HOTAIR --- MEG3 --- leukemia --- histone lysine methyltransferase --- RNA binding --- protein --- hydration --- wide-line 1H NMR --- secretion --- immune --- extracellular --- protein-protein interaction --- structural domain --- evolution --- transcription factors --- DNA-protein interactions --- Sox2 sequential DNA loading --- smFRET --- DNA conformational landscape --- sequential DNA bending --- transcription factor dosage --- oligomer --- N-terminal prion protein --- copper binding --- prion disease mutations --- Nuclear pore complex --- FG-Nups --- phosphorylation --- coarse-grained --- CABS model --- MC simulations --- statistical force fields --- protein structure --- intrinsically disordered proteins (IDPs) --- neurodegenerative diseases --- aggregation --- drugs --- drug discovery --- plant virus --- eIF4E --- VPg --- potyvirus --- molten globule --- fluorescence anisotropy --- protein hydrodynamics

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• Reference Manager
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• RefWorks (Direct export to RefWorks)

Disordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999. First, it was generally thought for more than a decade that disordered proteins or disordered parts of proteins have different amino acid compositions than folded proteins, and various prediction methods were developed based on this principle. These methods were suitable for distinguishing between the disordered (unstructured) and structured proteins known at that time. In addition, they could predict the site where a folded protein binds to the disordered part of a protein, shaping the latter into a well-defined 3D structure. Recently, however, evidence has emerged for a new type of disordered protein family whose members can undergo coupled folding and binding without the involvement of any folded proteins. Instead, they interact with each other, stabilizing their structure via “mutual synergistic folding” and, surprisingly, they exhibit the same residue composition as the folded protein. Increasingly more examples have been found where disordered proteins interact with non-protein macromolecules, adding to the already large variety of protein–protein interactions. There is also a very new phenomenon when proteins are involved in phase separation, which can represent a weak but functionally important macromolecular interaction. These phenomena are presented and discussed in the chapters of this book.

Research & information: general --- Biology, life sciences --- intrinsically disordered proteins --- epiproteome --- disordered protein platform --- molecular recognition feature --- post-translational modifications --- physiological homeostasis --- stress response --- RIN4 --- p53 --- molecular machines --- intrinsically disordered protein --- membrane-less organelle --- neurodegenerative disease --- p300 HAT acetylation --- post-translational modification --- protein aggregation --- Tau fibrillation --- intrinsically disorder proteins --- disorder-to-order regions --- protein–RNA interactions --- unstructured proteins --- conformational plasticity --- disordered protein --- folding --- ribosomal protein --- spectroscopy --- protein stability --- temperature response --- protein thermostability --- salt bridges --- meta strategy --- dual threshold --- significance voting --- decision tree based artificial neural network --- protein intrinsic disorder --- intrinsic disorder --- intrinsic disorder prediction --- intrinsically disordered region --- protein conformation --- transcriptome --- RNA sequencing --- Microarray --- differentially regulated genes --- gene ontology analysis --- functional analysis --- intrinsically disordered --- structural disorder --- correlated mutations --- co-evolution --- evolutionary couplings --- residue co-variation --- interaction surface --- residue contact network --- dehydron --- homodimer --- hydrogen bond --- inter-subunit interaction --- ion pair --- mutual synergistic folding --- solvent-accessible surface area --- stabilization center --- MLL proteins --- MLL4 --- lncRNA --- HOTAIR --- MEG3 --- leukemia --- histone lysine methyltransferase --- RNA binding --- protein --- hydration --- wide-line 1H NMR --- secretion --- immune --- extracellular --- protein-protein interaction --- structural domain --- evolution --- transcription factors --- DNA-protein interactions --- Sox2 sequential DNA loading --- smFRET --- DNA conformational landscape --- sequential DNA bending --- transcription factor dosage --- oligomer --- N-terminal prion protein --- copper binding --- prion disease mutations --- Nuclear pore complex --- FG-Nups --- phosphorylation --- coarse-grained --- CABS model --- MC simulations --- statistical force fields --- protein structure --- intrinsically disordered proteins (IDPs) --- neurodegenerative diseases --- aggregation --- drugs --- drug discovery --- plant virus --- eIF4E --- VPg --- potyvirus --- molten globule --- fluorescence anisotropy --- protein hydrodynamics --- intrinsically disordered proteins --- epiproteome --- disordered protein platform --- molecular recognition feature --- post-translational modifications --- physiological homeostasis --- stress response --- RIN4 --- p53 --- molecular machines --- intrinsically disordered protein --- membrane-less organelle --- neurodegenerative disease --- p300 HAT acetylation --- post-translational modification --- protein aggregation --- Tau fibrillation --- intrinsically disorder proteins --- disorder-to-order regions --- protein–RNA interactions --- unstructured proteins --- conformational plasticity --- disordered protein --- folding --- ribosomal protein --- spectroscopy --- protein stability --- temperature response --- protein thermostability --- salt bridges --- meta strategy --- dual threshold --- significance voting --- decision tree based artificial neural network --- protein intrinsic disorder --- intrinsic disorder --- intrinsic disorder prediction --- intrinsically disordered region --- protein conformation --- transcriptome --- RNA sequencing --- Microarray --- differentially regulated genes --- gene ontology analysis --- functional analysis --- intrinsically disordered --- structural disorder --- correlated mutations --- co-evolution --- evolutionary couplings --- residue co-variation --- interaction surface --- residue contact network --- dehydron --- homodimer --- hydrogen bond --- inter-subunit interaction --- ion pair --- mutual synergistic folding --- solvent-accessible surface area --- stabilization center --- MLL proteins --- MLL4 --- lncRNA --- HOTAIR --- MEG3 --- leukemia --- histone lysine methyltransferase --- RNA binding --- protein --- hydration --- wide-line 1H NMR --- secretion --- immune --- extracellular --- protein-protein interaction --- structural domain --- evolution --- transcription factors --- DNA-protein interactions --- Sox2 sequential DNA loading --- smFRET --- DNA conformational landscape --- sequential DNA bending --- transcription factor dosage --- oligomer --- N-terminal prion protein --- copper binding --- prion disease mutations --- Nuclear pore complex --- FG-Nups --- phosphorylation --- coarse-grained --- CABS model --- MC simulations --- statistical force fields --- protein structure --- intrinsically disordered proteins (IDPs) --- neurodegenerative diseases --- aggregation --- drugs --- drug discovery --- plant virus --- eIF4E --- VPg --- potyvirus --- molten globule --- fluorescence anisotropy --- protein hydrodynamics