Protein folding

Protein structure is determined by amino acid sequences. Learn about the four types of protein structures: primary, secondary, tertiary, and quaternary.

The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a…

The protein-folding problem is finally solved through DeepMind’s Alpha Fold.

Protein folding - Secondary structures

The folding funnel hypothesis is a specific version of the energy landscape theory of protein folding, which assumes that a protein's native state corresponds to its free energy minimum under the solution conditions usually encountered in cells. The folding funnel hypothesis assumes that the native state is a deep free energy minimum with steep walls, corresponding to a single well-defined tertiary structure.

Structural Biochemistry/Myoglobin - Wikibooks, open books for an open world

DeepMind's AI system AlphaFold cracked the so-called 'protein folding problem' - figuring out how a protein's amino acid sequence dictates its 3D atomic structure.

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Fluorescence has two distinct stages, excitation stage and emission stage. It is a phenomenon where fluorescent chromophore absorbs a light photon, typically remains in an excited state for a few nanoseconds and then emits a lower energy photon. Both the efficiency of light absorption (ε) and the efficiency of photon emission from an excited fluorophore (Q) determine the intensity of a sample. Changes in either ε and/or Q will lead to changes in sample emission intensity.