About

Professor Caitlin Davis is an Assistant Professor of Chemistry at Yale University, leading the Davis Lab established in 2020. Her research operates at the interface of biology, physics, and chemistry, with a focus on understanding the essential role of biodiversity in the adaptability and survival of cells. The lab's scientific endeavors emphasize the study of protein and RNA biophysics, live cell microscopy, spectroscopy, lasers, mathematical modeling, and physical chemistry. Professor Davis fosters an inclusive and diverse scholarly environment, valuing collaboration, communication, and respect for different perspectives. She actively recruits graduate and undergraduate students from diverse backgrounds to join her research group, tailoring projects to individual interests and expertise. The Davis Lab is committed to the principles of diversity, equity, and inclusion, which support both personal and intellectual growth in the pursuit of scientific excellence.

Research topics

• Biochemistry
• Biology
• Biophysics
• Chemistry
• Physical chemistry
• Internal medicine
• Medicine
• Chemical physics
• Computational chemistry
• Endocrinology
• Physics
• Stereochemistry

Selected publications

• Chemical interactions in polyethylene glycol-induced condensates lead to an anomalous FRET response from a flexible linker-fluorescent protein crowding sensor

  bioRxiv (Cold Spring Harbor Laboratory) · 2026-02-18

  articleOpen access

  The cellular cytosol is a crowded environment. Biomolecular Förster resonance energy transfer (FRET) sensors have been developed to measure crowding in cytosol mimics comprised of synthetic polymers such as polyethylene glycol (PEG) and Ficoll that impart an excluded volume effect. In the current study, we explore the unsolicited role of PEG in driving the phase separation of a protein crowding sensor, AcGFP1/mCherry-FRET crowding helix 2 (CrH2), into fluorescent puncta. In contrast, a DNA-based crowding sensor (CrD), with an Alexa488/Cy5 FRET pair, does not form puncta under the same crowding conditions. Using fluorescence recovery after photobleaching imaging, we uncover the liquid-like physical properties of the PEG-induced puncta. Two-color fluorescence microscopy imaging reveals crowder-induced inhomogeneity, concentration variations, and partition coefficient across the dilute and dense phases of the liquid puncta, which remain largely underexplored in bulk fluorometry measurements. Thus, the average crowding sensor response may originate from an aqueous biphasic system, reporting an erroneous average response instead of distinct levels of crowdedness. A comparison of excluded volume effects conferred by Ficoll and PEGs of various molecular weight ranges shows the influence of size, concentration, excluded volume, and chemical composition on the CrH2 sensor response. We demonstrate that PEGs enable phase separation and alter sensor response through a mechanism that may be driven by polymer interactions with the flexible hinge region of CrH2. Overall, we determine the biophysical mechanisms underlying PEG-induced condensation of CrH2 and demonstrate a CrD sensor as an alternative that does not undergo phase separation.

  PublisherDOI

• Mimetics of in-cell and subcellular crowding and solvation for protein folding

  Biochemical Society Transactions · 2026-04-01

  articleOpen accessSenior author

  Historically, fundamental principles of protein folding were extracted from dilute in vitro experiments that disregarded the complexity of the cell interior. It is now well-established that the cellular environment modulates protein behaviors. Discrepancies between protein properties measured in vitro and in-cell can be disentangled using mimetics that are designed to reproduce cellular interactions in vitro, steric crowding interactions and non-steric sticking interactions. Here, we review recent advances in the development and application of cellular mimetics of in-cell protein folding, with a focus on replicating diverse cell types and cellular compartments. Steric crowding interactions are typically mimicked using inert polymers; coupling these with giant unilamellar vesicles or phase separation allows for the creation of a cell- or organelle-like environment. Mimetics of non-steric chemical interactions must incorporate features of the chemical environment being mimicked. These range from buffers containing physiological concentrations of salt and small molecules to dilute lysates derived from the relevant cell type and/or organelle. Such mimetics of steric and non-steric interactions have greatly aided our understanding of in-cell protein folding. Mimetics can further approach biological accuracy through mixtures that simultaneously account for steric and non-steric interactions. Mimetic mixtures are important because they provide a convenient and cost-effective means to predict protein behavior in diverse cellular environments, which may benefit high-throughput applications, such as screening therapeutic candidates or training machine learning-based in-cell protein structure prediction models.

  PublisherDOI

• CCDC 2486055: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-02-19

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• Conformations and sequence determinants in the lipid binding of an adhesive peptide derived from Vibrio cholerae biofilms

  PLoS Pathogens · 2026-02-19

  articleOpen access

  Surface adhesion is critical to the survival of pathogenic bacteria both in natural niches and during infections, often via forming matrix-embedded communities called biofilms. Vibrio cholerae, the causal agent of pandemic cholera, is capable of forming biofilms adhering to both biotic and abiotic surfaces and the biofilm lifestyle has been implicated in promoting the survival of V. cholerae both in the natural reservoir and during host colonization. Previously, a 57-amino acid loop in the biofilm-specific adhesin Bap1 (Bap1-57aa) has been identified as a key contributor to the adhesion of V. cholerae biofilms to various surfaces including lipid membranes. However, the mechanism underlying its interaction with lipids, as well as its secondary structures, remain unresolved. Here, we combined biophysical, computational, and genetic approaches to elucidate the molecular mechanism of how this adhesive peptide interacts with lipids and lipid-coated surfaces. We found that a central aromatic-rich motif anchors the peptide to lipid bilayers while peripheral pseudo repeats enhance binding through avidity. Surprisingly, the core motif undergoes a lipid-induced conformational transition into a β-hairpin, enabling robust membrane insertion. We confirmed these findings both in vitro and in the biofilm context. Moreover, we demonstrated that the adhesive peptide can adhere to model host surfaces and is sensitive to membrane curvature. Finally, we show that the biofilm-derived peptide is found in several other Vibrio species, and its sequence is well-conserved. Our results provide molecular insight into biofilm adhesion and may lead to new strategies for targeted biofilm removal, as well as the design of bioinspired underwater adhesives.

  PublisherDOI

• CCDC 2486056: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-02-19

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• Anti-IL-15 treatment reduces acute lentivirus inflammation and signaling in the brain

  Cell Reports Medicine · 2026-01-01 · 1 citations

  articleOpen access

  infection display reduced neuroinflammation without altering brain viral burden. Peripheral IL-15 blockade decreases brain-infiltrating T lymphocytes, alters their spatial dynamics, suppresses proinflammatory cytokine (IL-6) expression in microglia, and increases anti-inflammatory cytokine (TGF-β) expression in brain macrophages. Transcriptomic profiling reveals a global reduction in inflammatory signaling and an upregulation of genes associated with M1 macrophage pathways. Together, these findings demonstrate that peripheral IL-15 modulation attenuates neuroinflammation during acute lentiviral infection and highlight IL-15 as a potential therapeutic target for neuroinflammatory conditions of the brain.

  PublisherDOI

• CCDC 2486058: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-02-19

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

• BPS2026 – Chemical interactions in polyethylene glycol-induced phase separation lead to an anomalous FRET response from a flexible linker-fluorescent protein crowding sensor

  Biophysical Journal · 2026-02-01

  article
  PublisherDOI

• Photopatternable Thermochromism Enabled by an Anthracene Heterodimer Ligand

  Journal of the American Chemical Society · 2026-02-13

  article

  Shortwave ultraviolet light retrocyclizes anthracene dimers (dianthracenes) to their corresponding monomers in the solid state, changing their solubility, fluorescence, geometry, conjugation, covalency, and more. Dianthracenes are thus an ideal building block for intrinsically photopatternable functional materials with bespoke optical, electronic, and magnetic properties. Here we present a new strategy to prepare such materials based on a "heterodimer" of anthracene and 9,10-anthracenedicarboxylic acid that allows us to photopattern the thermochromic phase of a Cu MOF in a two-dimensional (2D)-to-2D transformation, i.e., without dimensional reduction. The thermochromic phase can also be accessed by thermal annealing, as the 2D-to-2D nature of the structural transformation prevents melting. Upon retrocyclization, the parent anthracene released from our heterodimer deintercalates from between the 2D sheets, resulting in a massive, highly anisotropic structural rearrangement and remarkable 44% mass loss without crystal destruction. Furthermore, we demonstrate that 4-substituents on the pyridine ligands can be used to tune the thermochromism, which is based on thermal population of the triplet excited state of a Cu paddlewheel dimer.

  PublisherDOI

• CCDC 2486057: Experimental Crystal Structure Determination

  The Cambridge Structural Database · 2026-02-19

  datasetOpen access

  An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

  PublisherDOI

Recent grants

• Protein Structural Dynamics in Living Cells

  NIH · $1.3M · 2023–2028

Frequent coauthors

• Martin Gruebele

  21 shared

• R. Brian Dyer

  13 shared

• Sydney O. Shuster

  10 shared

• Amanda J. Martinot

  6 shared

• Dan H. Barouch

  Harvard University

  6 shared

• R. Keith Reeves

  Duke University

  6 shared

• Chen Tan

  Hebei General Hospital

  5 shared

• Edward Knab

  Yale University

  5 shared

Labs

• Davis LabPI

Education

• Ph.D., Chemistry

  Emory University

  2015

• BS, Chemistry and Mathematics

  University of Michigan

  2007

Awards & honors

• Beckman Young Investigator (2024-2028)
• National Science Foundation Faculty Early Career Development…
• Hevolution/AFAR New Investigator Awards in Aging Biology and…
• Scialog Fellow (2019-2021)
• Center for the Physics of Living Cells Postdoctoral Fellowsh…