Toolkit/quantum chemical calculations

quantum chemical calculations

Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.

Usefulness & Problems

No literature-backed usefulness or problem-fit explainer has been materialized for this record yet.

Published Workflows

Objective: Study structural changes and molecular mechanisms in light-sensitive proteins following photoexcitation by integrating experimental structural measurements with computational analysis.

Why it works: The review explicitly frames recent progress as coming from combining time-resolved crystallography at XFELs with quantum chemical calculations, implying complementary experimental and computational views of photoinduced structural dynamics.

photoexcitation-driven structural changetime-resolved crystallographyX-ray free electron laser measurementsquantum chemical calculations

Taxonomy & Function

Primary hierarchy

Technique Branch

Method: A concrete computational method used to design, rank, or analyze an engineered system.

Target processes

No target processes tagged yet.

Input: Light

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1capability summarysupports2022Source 1needs review

Structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.

The structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.
Claim 2review scope summarysupports2022Source 1needs review

Recent progress has combined time-resolved crystallography at X-ray free electron lasers with quantum chemical calculations to study structural changes in light-sensitive proteins following photoexcitation.

Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.

Approval Evidence

1 source2 linked approval claimsfirst-pass slug quantum-chemical-calculations
Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.

Source:

capability summarysupports

Structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.

The structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.

Source:

review scope summarysupports

Recent progress has combined time-resolved crystallography at X-ray free electron lasers with quantum chemical calculations to study structural changes in light-sensitive proteins following photoexcitation.

Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.

Source:

Comparisons

No literature-backed comparison notes have been materialized for this record yet.

Ranked Citations

  1. 1.
    StructuralSource 1Current Opinion in Structural Biology2022Claim 1Claim 2

    Seeded from load plan for claim cl1. Extracted from this source document.