Inês S. Camacho

ORCID: 0000-0001-9351-8981
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About
Contact & Profiles
Research Areas
  • Photosynthetic Processes and Mechanisms
  • Enzyme Structure and Function
  • Light effects on plants
  • Protein Structure and Dynamics
  • Porphyrin Metabolism and Disorders
  • Folate and B Vitamins Research
  • Photoreceptor and optogenetics research
  • Plant Molecular Biology Research
  • Protein purification and stability
  • Retinal Development and Disorders
  • DNA Repair Mechanisms
  • Heme Oxygenase-1 and Carbon Monoxide
  • DNA and Nucleic Acid Chemistry
  • Cancer Research and Treatments

National Physical Laboratory
2018-2023

University of Manchester
2018-2021

Czech Academy of Sciences, Institute of Biotechnology
2018

Rede de Química e Tecnologia
2014

Universidade Nova de Lisboa
2014

Significance The plant photoreceptor UVR8 absorbs UV-B light to regulate UV protection and photomorphogenic responses in plants. Here we show that adopts multiple conformations generate the signaling active state. conformational diversity of was revealed using a native mass spectrometry approach, where photoactivated ion source. Our analyses not only disordered but also ostensibly well-folded regions can adopt highly extended are likely enhance interactions with partner proteins facilitate...

10.1073/pnas.1813254116 article EN cc-by Proceedings of the National Academy of Sciences 2019-01-04

Structure-function relationships of biological macromolecules, in particular proteins, provide crucial insights for fundamental biochemistry, medical research and early drug discovery. However, production recombinant either structure determination, functional studies, or to be used as biopharmaceutical products, is often hampered by their instability propensity aggregate solution vitro. Protein samples poor quality are associated with reduced reproducibility well high expenses. Several...

10.3389/fmolb.2022.890862 article EN cc-by Frontiers in Molecular Biosciences 2022-05-16

Optogenetic actuators have revolutionized the resolution at which biological processes can be controlled. In plants, deployment of optogenetics is challenging due to need for these light-responsive systems function in context horticultural light environments. Furthermore, many available optogenetic are based on plant photoreceptors that might crosstalk with endogenous signaling processes, while others depend exogenously supplied cofactors. To overcome such challenges, we developed...

10.1371/journal.pbio.3002303 article EN cc-by PLoS Biology 2023-09-21

The function of the bacterial photoreceptor protein, CarH, is regulated by changes to its oligomeric state. Camacho <italic>et al.</italic> detail how binding vitamin B<sub>12</sub> in dark drives assembly protein tetramer that turn blocks transcription.

10.1039/d1sc00522g article EN cc-by Chemical Science 2021-01-01

Time-resolved infrared spectroscopy reveals the flow of electron density through coenzyme B12 in light-activated, bacterial transcriptional regulator, CarH. The protein stabilises a series charge transfer states that result photoresponse avoids reactive, and potentially damaging, radical photoproducts.

10.1039/d3cc03900e article EN Chemical Communications 2023-01-01

It is now over 30 years since Demchenko and Ladokhin first posited the potential of tryptophan red edge excitation shift (REES) effect to capture information on protein molecular dynamics. While there have been many key efforts in intervening years, a biophysical thermodynamic model quantify relationship between REES flexibility has lacking. Without such full cannot be realized. Here, we present that captures conformational flexibility, even with proteins containing multiple residues. Our...

10.3389/fmolb.2021.778244 article EN Frontiers in Molecular Biosciences 2021-12-03

Abstract UVR8 is a plant photoreceptor protein that regulates photomorphogenic and protective responses to UV light. The inactive, homodimeric state absorbs UV-B light resulting in dissociation into monomers, which are considered be the active comprise β-propeller core domain intrinsically disordered N- C-terminal tails. C-terminus required for functional binding signalling partner COP1. To date, however, structural studies have only been conducted with where terminal tails truncated. Here,...

10.1101/371658 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2018-07-18

Time-resolved infrared spectroscopy reveals the flow of electron density through coenzyme B 12 in light-activated, bacterial transcriptional regulator, CarH. The protein stabilises a series charge transfer states that result photoresponse avoids reactive, and potentially damaging, radical photoproducts.

10.1101/2023.08.11.552799 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2023-08-14

Abstract Optogenetic actuators have revolutionized the resolution at which we can assert control over biological processes in living systems. In plants, deployment of optogenetics is challenging due to need for these light-responsive systems maintain a single activation state conventional horticultural environments with light-dark cycling. Furthermore, many available optogenetic are based on plant photoreceptors that might crosstalk endogenous signaling processes, while others depend...

10.1101/2022.10.28.514161 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-10-29

ABSTRACT It is now over thirty years since Demchenko and Ladokhin first posited the potential of tryptophan red edge excitation shift (REES) effect to capture information on protein molecular dynamics. Whilst there have been many key efforts in intervening years, a biophysical thermodynamic model quantify relationship between REES flexibility has lacking. Without such full cannot be realized. Here, we present that captures conformational flexibility, even with proteins containing multiple...

10.1101/2021.09.09.459605 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-09-09
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