By integrating two methodologies, scholars have uncovered the critical function of ‘coherence’ in molecular reactions, thereby establishing a foundation for the sophisticated manipulation of molecular dynamics. The process has been visually depicted. Credit: Samuel Perrett
Utilizing ultrafast physics within the domain of structural biology, researchers have provided a detailed depiction of molecular ‘coherence’ as never seen before.
Grasping the transformations that molecules undergo in reaction to external factors like light is vital in biological processes, including photosynthesis. Scientific research across multiple domains has been devoted to decoding these molecular changes. By amalgamating two such areas, scientists have laid the groundwork for an innovative phase in comprehending the essential protein molecule reactions that sustain life.
A distinguished international research team led by Professor Jasper van Thor of Imperial’s Department of Life Sciences has recently published their results in the academic journal, Nature Chemistry.
Crystallography, a pivotal methodology in structural biology, allows for the capturing of ‘snapshots’ that display the arrangement of molecules. Over the course of extensive experiments and theoretical research spanning several years, the authors of the new study successfully combined this with spectroscopy, another technique that identifies molecular vibrations in electronic and nuclear configurations.
Employing the newly developed method at state-of-the-art X-ray laser installations globally, the researchers demonstrated that the initial movements in optically excited molecules within a studied protein are attributable to ‘coherence,’ which manifests as vibrational activity rather than functional biological reactions.
This groundbreaking distinction, empirically validated for the first time, underscores how spectroscopic physics can augment the traditional methods of structural biology grounded in crystallography.
Professor van Thor commented, “Processes that sustain life are mediated by proteins. Comprehending their complex functionality hinges on deciphering their atomic structure and its subsequent changes during reactions. Employing spectroscopic methodologies now enables us to directly visualize ultrafast molecular movements pertaining to the coherence process by resolving their crystal structures. This provides us with the instrumentation to analyze, and potentially control, molecular dynamics on extraordinarily rapid timescales with near-atomic precision.”
The research involved extensive utilization of X-ray free-electron laser (XFEL) facilities, including several globally recognized institutions. Team members have been actively exploring protein reactions on the femtosecond scale since 2009. X-rays are employed to capture ‘snapshots’ of the molecular structure following excitation by a laser pulse.
The study, a culmination of seven years of interdisciplinary work involving 49 authors from 15 institutions, contributes significant advancements to both time-resolved structural biology and ultrafast laser spectroscopy. The meticulous experiments and theoretical interpretations demonstrate that ultrafast molecular movements, precisely measured on the femtosecond timescale and picometer scale, are not part of biological reactions but belong to vibrational coherence in the remaining ground state.
Professor van Thor added, “The study confirms that traditional time-resolved measurements are dominated by ground state motions unrelated to light-triggered biological reactions. These findings were anticipated in theoretical literature but have now been verified experimentally, marking a notable impact in both related scientific fields.”
The collaborative effort, which even included remote work during the pandemic, proved instrumental in achieving these results. Co-authors from various prestigious institutions echoed the sentiment that the study showcases the unique capabilities of X-ray lasers in advancing our knowledge of biological processes in motion.
Reference: “Optical control of ultrafast structural dynamics in a fluorescent protein,” authored by an extensive team of researchers and led by Jasper J. van Thor, was published on 10 August 2023 in Nature Chemistry. DOI: 10.1038/s41557-023-01275-1.
Table of Contents
Frequently Asked Questions (FAQs) about Molecular Coherence
What is the main focus of the research described in the article?
The primary focus of the research is to understand the role of ‘coherence’ in molecular reactions. By combining two methodologies—crystallography and spectroscopy—researchers have achieved unprecedented clarity in depicting molecular coherence. This work lays the foundation for advanced manipulation and understanding of molecular dynamics.
Who led the research team?
The international research team was led by Professor Jasper van Thor from the Department of Life Sciences at Imperial College London. Their findings were recently published in the journal Nature Chemistry.
What techniques were integrated in the study?
The study integrated crystallography and spectroscopy to achieve its results. Crystallography provides ‘snapshots’ of molecular arrangements, while spectroscopy identifies vibrations in electronic and nuclear configurations of molecules.
What are the practical applications of this research?
The research has practical implications in various scientific domains, particularly structural biology and ultrafast laser spectroscopy. It provides tools for understanding and potentially controlling molecular dynamics on extremely rapid timescales with near-atomic precision.
Was the research collaborative?
Yes, the research was highly collaborative, involving 49 authors from 15 different institutions. It is the culmination of seven years of interdisciplinary work, which even included experiments conducted remotely during the pandemic.
What did the research conclude about ultrafast molecular movements?
The research concluded that ultrafast molecular movements, precisely measured on both the femtosecond timescale and picometer scale, are attributable to vibrational coherence in the remaining ground state. These movements are not part of the biological reactions but belong to what is traditionally measured by vibrational spectroscopy.
What facilities were used for the research?
The research extensively utilized X-ray free-electron laser (XFEL) facilities. These included globally recognized institutions such as the Linac Coherent Light Source (LCLS) in the USA, SPring-8 Angstrom Compact free electron LAser (SACLA) in Japan, PAL-XFEL in Korea, and the European XFEL in Hamburg.
How is this research groundbreaking?
This research is groundbreaking because it empirically validates, for the first time, the role of ‘coherence’ in molecular reactions. It advances our understanding of molecular dynamics and sets the stage for future investigations in related scientific fields.
More about Molecular Coherence
- Nature Chemistry Journal
- Department of Life Sciences, Imperial College London
- Linac Coherent Light Source
- SPring-8 Angstrom Compact free electron LAser (SACLA)
- PAL-XFEL in Korea
- European XFEL in Hamburg
- Structural Biology Overview
- Ultrafast Laser Spectroscopy
- Crystallography in Biology
8 comments
So they’re using lasers now to understand proteins? Man, we live in the future.
If we can understand the coherence in molecular dynamics, think of the applications! Maybe we can finally figure out more about the biological processes on a molecular lvl.
Femtochemistry? I’m in. We’re literally talking about one-millionth of one billionth of a second. Can’t get my head around that.
Its not just the scientific breakthrough that’s impressive. Its the international effort and 7-year dedication. Incredible.
Wow, this is a game-changer. Can’t believe how far we’ve come in understanding molecular reactions. Science is just mind-blowing sometimes.
Honestly, this could revolutionize medicine too. Understanding proteins at this level is huge for drug design.
i thought crystallography was complex enough, but mixing it with spectroscopy? That’s next level, hats off to Prof. van Thor and his team.
49 authors from 15 institutions? That’s what I call collaboration. Science is a team sport, folks.