Estructura de las proteínas. Mezclando en esta cuerda mortal.

Overview of protein folding.

Current protocols in protein science·2008

Quantitative analysis of the stabilization by substrate of Staphylococcus aureus PC1 beta-lactamase.

Chemistry & biology·2001

A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin.

European journal of biochemistry·2001

The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme.

Biochemistry·2000

Location of the binding site for chloride ion activation of cathepsin C.

European journal of biochemistry·1999

Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibition.

Biochemical and biophysical research communications·1999

Universal gates from braiding and fusing anyons on quantum hardware.

Nature·2026

People use fast and flat simulation to reason about new games.

Nature·2026

Rising dust pollution across Europe in a changing climate.

Nature·2026

Ammonia pressure controls colloidal metal nitride synthesis in molten salts.

Nature·2026

Programming fracture resistance in metamaterials via elastic instabilities.

Nature·2026

Selectivity Emerges from Indiscriminate Photoreduction.

Nature·2026

Interfacial Charge-Driven Compression-Induced Structural and Morphological Reorganization in Lysozyme-DMPA Mixed Langmuir Films.

The journal of physical chemistry. B·2026

Synaptic Ca2+ channels and neurexins are linked through direct and indirect binding complexes.

Scientific reports·2026

Highly Dynamic Yet Stable Polyketimine Networks with Closed-Loop Recyclability and Topological Programmability.

Journal of the American Chemical Society·2026

Recent Progress in Coupling Reactions Involving the Novel Substrate of Bicyclo[1.1.0]butane (BCB).

Topics in current chemistry (Cham)·2026

Coupling of Electrostatic Interactions and Electroosmotic Flow in the Translocation of a Single-Stranded RNA through Charged Nanopores.

The journal of physical chemistry. B·2026

Direct interaction between tubulin and PMCA, a complex with functional implications.

FEBS letters·2026

Videos de Experimentos Relacionados

Estructura de las proteínas. Mezclando en esta cuerda mortal.

Videos de Conceptos Relacionados

Overview of protein folding.

Quantitative analysis of the stabilization by substrate of Staphylococcus aureus PC1 beta-lactamase.

A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin.

The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme.

Location of the binding site for chloride ion activation of cathepsin C.

Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibition.

Universal gates from braiding and fusing anyons on quantum hardware.

People use fast and flat simulation to reason about new games.

Rising dust pollution across Europe in a changing climate.

Ammonia pressure controls colloidal metal nitride synthesis in molten salts.

Programming fracture resistance in metamaterials via elastic instabilities.

Selectivity Emerges from Indiscriminate Photoreduction.

Interfacial Charge-Driven Compression-Induced Structural and Morphological Reorganization in Lysozyme-DMPA Mixed Langmuir Films.

Synaptic Ca2+ channels and neurexins are linked through direct and indirect binding complexes.

Highly Dynamic Yet Stable Polyketimine Networks with Closed-Loop Recyclability and Topological Programmability.

Recent Progress in Coupling Reactions Involving the Novel Substrate of Bicyclo[1.1.0]butane (BCB).

Coupling of Electrostatic Interactions and Electroosmotic Flow in the Translocation of a Single-Stranded RNA through Charged Nanopores.

Direct interaction between tubulin and PMCA, a complex with functional implications.

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Estructura de las proteínas. Mezclando en esta cuerda mortal.

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