Search Results - "proteins"

Fuzzy protein theory for disordered proteins

Table of Contents: “…Contents: Intelligent decision-making mechanisms -- Structural disorder is maintained in protein assemblies -- Mechanisms and biological consequences of fuzziness -- Conformational diversity and context-dependence -- Fuzziness in cell differentiation and transcription factor evolution -- Material state and regulation of higher-order assemblies.…”
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Fuzzy protein theory for disordered proteins

Table of Contents: “…Contents: Intelligent decision-making mechanisms -- Structural disorder is maintained in protein assemblies -- Mechanisms and biological consequences of fuzziness -- Conformational diversity and context-dependence -- Fuzziness in cell differentiation and transcription factor evolution -- Material state and regulation of higher-order assemblies.…”
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Fuzzy protein theory for disordered proteins

Table of Contents: “…Contents: Intelligent decision-making mechanisms -- Structural disorder is maintained in protein assemblies -- Mechanisms and biological consequences of fuzziness -- Conformational diversity and context-dependence -- Fuzziness in cell differentiation and transcription factor evolution -- Material state and regulation of higher-order assemblies.…”
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Protein folding

Table of Contents: “…Contents: Introduction to principles of protein structure -- The basic facts about protein folding -- Cooperativity of protein structure formation -- Necessary and sufficient conditions for protein sequences to fold -- Concept of energy gap -- Protein folding kinetics -- Intermediates and transition state ensembles -- Allatom folding simulations -- Understanding protein folding pathways at atomic detail.…”
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Protein folding

Table of Contents: “…Contents: Introduction to principles of protein structure -- The basic facts about protein folding -- Cooperativity of protein structure formation -- Necessary and sufficient conditions for protein sequences to fold -- Concept of energy gap -- Protein folding kinetics -- Intermediates and transition state ensembles -- Allatom folding simulations -- Understanding protein folding pathways at atomic detail.…”
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Protein folding

Table of Contents: “…Contents: Introduction to principles of protein structure -- The basic facts about protein folding -- Cooperativity of protein structure formation -- Necessary and sufficient conditions for protein sequences to fold -- Concept of energy gap -- Protein folding kinetics -- Intermediates and transition state ensembles -- Allatom folding simulations -- Understanding protein folding pathways at atomic detail.…”
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Aging and protein homeostasis

Table of Contents: “…Contents: Aging and protein homeostasis -- What is the role of proteotoxicity in aging? …”
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Series (Autophagy and lysosomal storage diseases)
Series (Aging)

Intrinsically unstructured proteins regulation and disease /

Table of Contents: “…Contents: Regulatory genomics and systems biology -- Intrinsically unstructured proteins (IUPs): structural and biophysical advantage -- Functional advantage -- Thermodynamic and kinetic advantage -- Conformational advantage -- Identification of IUPs -- Functions of IUPs -- Disadvantages of unstructured regions -- Unstructured regions in proteins -- Cells minimize the risks of unstructured proteins -- Tight regulation of IUPs -- Key regulatory events affecting protein availability -- IUPs in yeast -- Gene-ontology functional enrichment analysis -- Genome-scale datasets on transcript availability -- Transcripts encoding IUPs are tightly controlled -- Mechanisms affecting transcript stability -- Genome-scale datasets on protein availability -- IUPs are tightly controlled at the translational level -- PEST sequences -- Aggregation prone IUPs: more tightly regulated -- Control calculation -- Tight regulation of IUPs is evolutionarily conserved -- Control of IUP affects signaling fidelity/regulation -- Control of specific IUP affects protein aggregation.…”
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The unfolded protein response

Table of Contents: “…Contents: Molecular mechanism unfolded protein response -- Physiological importance of the unfolded protein response -- Intracellular signaling from the endoplasmic reticulum (ER) to the nucleus -- Reasons for activation -- Maintenance of homeostasis of the ER.…”
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Protein folding in vivo

Table of Contents: “…Contents: Protein folding in vivo -- Protein folding as facilitated by the acid inducible chaperone HdeA -- Optimization of folding in vivo illustrates a tradeoff between stability and function -- The Spy chaperone.…”
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Protein folding and misfolding from theory to therapy /

Table of Contents: “…Contents: Protein nature, folding and complexity -- Folding in a cellular environment -- The underlying principles of folding -- Native and transition states -- Exploring the energy surface -- The folding of lysozyme -- The consequences of protein misfolding -- The relationship between folding and disease -- Protein deposition diseases -- Protein aggregates in amyloid diseases -- Amyloidogenic mutations of lysozyme -- Mechanism of amyloid formation -- Structure of the amyloidogenic intermediate -- Amyloid formation by lysozyme in vivo -- SH3 domain of PI3 kinase -- Model of an amyloid fibril -- The underlying origins of amyloid disease -- Generic toxicity of amyloid aggregates -- Cellular defences against aggregation -- Evolutionary design of proteins -- "Post-evolutionary" diseases.…”
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Protein stability and folding

Table of Contents: “…Contents: Protein stability -- Folding and refolding -- Molecular chaperones -- Motions within proteins -- Protein classification by function -- Protein classification by complexity.…”
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Aging and protein homeostasis

Table of Contents: “…Contents: Aging and protein homeostasis -- What is the role of proteotoxicity in aging? …”
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Series (Autophagy and lysosomal storage diseases)
Series (Aging)

Intrinsically unstructured proteins regulation and disease /

Table of Contents: “…Contents: Regulatory genomics and systems biology -- Intrinsically unstructured proteins (IUPs): structural and biophysical advantage -- Functional advantage -- Thermodynamic and kinetic advantage -- Conformational advantage -- Identification of IUPs -- Functions of IUPs -- Disadvantages of unstructured regions -- Unstructured regions in proteins -- Cells minimize the risks of unstructured proteins -- Tight regulation of IUPs -- Key regulatory events affecting protein availability -- IUPs in yeast -- Gene-ontology functional enrichment analysis -- Genome-scale datasets on transcript availability -- Transcripts encoding IUPs are tightly controlled -- Mechanisms affecting transcript stability -- Genome-scale datasets on protein availability -- IUPs are tightly controlled at the translational level -- PEST sequences -- Aggregation prone IUPs: more tightly regulated -- Control calculation -- Tight regulation of IUPs is evolutionarily conserved -- Control of IUP affects signaling fidelity/regulation -- Control of specific IUP affects protein aggregation.…”
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The unfolded protein response

Table of Contents: “…Contents: Molecular mechanism unfolded protein response -- Physiological importance of the unfolded protein response -- Intracellular signaling from the endoplasmic reticulum (ER) to the nucleus -- Reasons for activation -- Maintenance of homeostasis of the ER.…”
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Series

Protein folding in vivo

Table of Contents: “…Contents: Protein folding in vivo -- Protein folding as facilitated by the acid inducible chaperone HdeA -- Optimization of folding in vivo illustrates a tradeoff between stability and function -- The Spy chaperone.…”
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Series

Protein folding and misfolding from theory to therapy /

Table of Contents: “…Contents: Protein nature, folding and complexity -- Folding in a cellular environment -- The underlying principles of folding -- Native and transition states -- Exploring the energy surface -- The folding of lysozyme -- The consequences of protein misfolding -- The relationship between folding and disease -- Protein deposition diseases -- Protein aggregates in amyloid diseases -- Amyloidogenic mutations of lysozyme -- Mechanism of amyloid formation -- Structure of the amyloidogenic intermediate -- Amyloid formation by lysozyme in vivo -- SH3 domain of PI3 kinase -- Model of an amyloid fibril -- The underlying origins of amyloid disease -- Generic toxicity of amyloid aggregates -- Cellular defences against aggregation -- Evolutionary design of proteins -- "Post-evolutionary" diseases.…”
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Series

Protein folding and misfolding from theory to therapy /

Table of Contents: “…Contents: Protein nature, folding and complexity -- Folding in a cellular environment -- The underlying principles of folding -- Native and transition states -- Exploring the energy surface -- The folding of lysozyme -- The consequences of protein misfolding -- The relationship between folding and disease -- Protein deposition diseases -- Protein aggregates in amyloid diseases -- Amyloidogenic mutations of lysozyme -- Mechanism of amyloid formation -- Structure of the amyloidogenic intermediate -- Amyloid formation by lysozyme in vivo -- SH3 domain of PI3 kinase -- Model of an amyloid fibril -- The underlying origins of amyloid disease -- Generic toxicity of amyloid aggregates -- Cellular defences against aggregation -- Evolutionary design of proteins -- "Post-evolutionary" diseases.…”
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Series

The unfolded protein response

Table of Contents: “…Contents: Molecular mechanism unfolded protein response -- Physiological importance of the unfolded protein response -- Intracellular signaling from the endoplasmic reticulum (ER) to the nucleus -- Reasons for activation -- Maintenance of homeostasis of the ER.…”
Get full text
Series

Protein folding in vivo

Table of Contents: “…Contents: Protein folding in vivo -- Protein folding as facilitated by the acid inducible chaperone HdeA -- Optimization of folding in vivo illustrates a tradeoff between stability and function -- The Spy chaperone.…”
Get full text
Series