Hydrogen Atoms Are Produced When Tryptophan within a Protein Is Irradiated with Ultraviolet Light

Angiolillo, Paul J.; Vanderkooi, Jane M.

doi:10.1111/j.1751-1097.1996.tb03095.x

Cited by 9 publications

(6 citation statements)

References 40 publications

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“…15 (iv) It has been shown, in good agreement with this mechanism, that H atoms are produced when tryptophan is irradiated with ultraviolet light within a protein. 35 (v) Our model predicts the formation of hydrated electrons as transient species in the H-transfer reaction in aqueous environment. This effect has been observed for numerous aromatic chromophores upon UV excitation in water 36 and indole and Trp are among the best known examples.…”

Section: Introductionmentioning

confidence: 89%

External electric field effect on the lowest excited states of indole: ab initio and molecular dynamics study

Dedonder‐Lardeux

Jouvet

Perun

et al. 2003

Phys. Chem. Chem. Phys.

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Section: Introductionmentioning

confidence: 89%

External electric field effect on the lowest excited states of indole: ab initio and molecular dynamics study

Dedonder‐Lardeux

Jouvet

Perun

et al. 2003

Phys. Chem. Chem. Phys.

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“…Trp and Tyr are responsible for most of the characteristic protein UV absorbance at 280 nm . Trp is also responsible for most intrinsic protein fluorescence. , These unique features allow Trp residues to be photoactivated under UV irradiation. − In brief, Trp under irradiation by UV light results in a tryptophan radical and a hydrated electron. ,, The formation of tryptophan radical-mediated reactive oxidative species leads to hydrogen peroxide as a product, , which further oxidizes nearby residues . A recent book by Lundblad provides a detailed overview of Trp photoactivation.…”

Section: Targeted-labeling Reagentsmentioning

confidence: 99%

Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications

2020

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Proteins adopt different higher-order structures (HOS) to enable their unique biological functions. Understanding the complexities of protein higher-order structures and dynamics requires integrated approaches, where mass spectrometry (MS) is now positioned to play a key role. One of those approaches is protein footprinting. Although the initial demonstration of footprinting was for the HOS determination of protein/nucleic acid binding, the concept was later adapted to MS-based protein HOS analysis, through which different covalent labeling approaches “mark” the solvent accessible surface area (SASA) of proteins to reflect protein HOS. Hydrogen–deuterium exchange (HDX), where deuterium in D2O replaces hydrogen of the backbone amides, is the most common example of footprinting. Its advantage is that the footprint reflects SASA and hydrogen bonding, whereas one drawback is the labeling is reversible. Another example of footprinting is slow irreversible labeling of functional groups on amino acid side chains by targeted reagents with high specificity, probing structural changes at selected sites. A third footprinting approach is by reactions with fast, irreversible labeling species that are highly reactive and footprint broadly several amino acid residue side chains on the time scale of submilliseconds. All of these covalent labeling approaches combine to constitute a problem-solving toolbox that enables mass spectrometry as a valuable tool for HOS elucidation. As there has been a growing need for MS-based protein footprinting in both academia and industry owing to its high throughput capability, prompt availability, and high spatial resolution, we present a summary of the history, descriptions, principles, mechanisms, and applications of these covalent labeling approaches. Moreover, their applications are highlighted according to the biological questions they can answer. This review is intended as a tutorial for MS-based protein HOS elucidation and as a reference for investigators seeking a MS-based tool to address structural questions in protein science.

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“…Serotonin (5HT) projections to the BG are also known to have an important role in decision making (Rogers, 2011). 5HT is an ancient molecule that existed even in plants (Angiolillo and Vanderkooi, 1996). Through its precursor tryptophan, 5HT is linked to some of the fundamental processes of life itself.…”

Section: Introductionmentioning

confidence: 99%

“…Through its precursor tryptophan, 5HT is linked to some of the fundamental processes of life itself. Tryptophan-based molecules in plants are crucial for capturing the light energy necessary for glucose metabolism and oxygen production (Angiolillo and Vanderkooi, 1996). Thus, by virtue of its fundamental role in energy conversion, 5HT is integral to mitosis, maturation, and apoptosis.…”

Section: Introductionmentioning

confidence: 99%

An extended reinforcement learning model of basal ganglia to understand the contributions of serotonin and dopamine in risk-based decision making, reward prediction, and punishment learning

Balasubramani¹,

Chakravarthy²,

Ravindran³

et al. 2014

Front. Comput. Neurosci.

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Although empirical and neural studies show that serotonin (5HT) plays many functional roles in the brain, prior computational models mostly focus on its role in behavioral inhibition. In this study, we present a model of risk based decision making in a modified Reinforcement Learning (RL)-framework. The model depicts the roles of dopamine (DA) and serotonin (5HT) in Basal Ganglia (BG). In this model, the DA signal is represented by the temporal difference error (δ), while the 5HT signal is represented by a parameter (α) that controls risk prediction error. This formulation that accommodates both 5HT and DA reconciles some of the diverse roles of 5HT particularly in connection with the BG system. We apply the model to different experimental paradigms used to study the role of 5HT: (1) Risk-sensitive decision making, where 5HT controls risk assessment, (2) Temporal reward prediction, where 5HT controls time-scale of reward prediction, and (3) Reward/Punishment sensitivity, in which the punishment prediction error depends on 5HT levels. Thus the proposed integrated RL model reconciles several existing theories of 5HT and DA in the BG.

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Hydrogen Atoms Are Produced When Tryptophan within a Protein Is Irradiated with Ultraviolet Light

Cited by 9 publications

References 40 publications

External electric field effect on the lowest excited states of indole: ab initio and molecular dynamics study

External electric field effect on the lowest excited states of indole: ab initio and molecular dynamics study

Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications

An extended reinforcement learning model of basal ganglia to understand the contributions of serotonin and dopamine in risk-based decision making, reward prediction, and punishment learning

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