Model of a protein, antigen 85B, that is the most abundant protein exported by Mycobacterium tuberculosis, which causes most cases of tuberculosis. Antigen 85B is involved in building the bacterial cell wall and is an attractive drug target. Based on its structure, scientists have suggested a new class of antituberculous drugs.

CellPack image of the H1N1 influenza virus, with hemagglutinin and neuraminidase glycoproteins in green and red, respectively, on the outer envelope (white); matrix protein in gray, and ribonucleoprotein particles inside the virus in red and green. Related to image 6356.

Meiosis is used to make sperm and egg cells. During meiosis, a cell's chromosomes are copied once, but the cell divides twice. During mitosis, the chromosomes are copied once, and the cell divides once. For simplicity, cells are illustrated with only three pairs of chromosomes.

See image 1333 for an unlabeled version of this illustration.

Phenylalanine tRNA showing the anticodon (yellow) and the amino acid, phenylalanine (blue and red spheres).

A 3D reconstruction, created using cryo-electron microscopy, of an ion channel known as the full-length serotonin receptor in complex with the antinausea drug granisetron (orange). Ion channels are proteins in cell membranes that help regulate many processes.

This image is a computer-generated model of the approximately 4.2 million atoms of the HIV capsid, the shell that contains the virus' genetic material. Scientists determined the exact structure of the capsid and the proteins that it's made of using a variety of imaging techniques and analyses. They then entered these data into a supercomputer that produced the atomic-level image of the capsid. This structural information could be used for developing drugs that target the capsid, possibly leading to more effective therapies. Related to image 6601.

Acetylsalicylate (bottom) is the aspirin of today. Adding a chemical tag called an acetyl group (shaded box, bottom) to a molecule derived from willow bark (salicylate, top) makes the molecule less acidic (and easier on the lining of the digestive tract), but still effective at relieving pain. See image 2529 for an unlabeled version of this illustration. Featured in Medicines By Design.

Developing spermatids (precursors of mature sperm cells) begin as small, round cells and mature into long-tailed, tadpole-shaped ones. In the sperm cell's head is the cell nucleus; in its tail is the power to outswim thousands of competitors to fertilize an egg. As seen in this microscopy image, fruit fly spermatids start out as groups of interconnected cells. A small lipid molecule called PIP2 helps spermatids tell their heads from their tails. Here, PIP2 (red) marks the nuclei and a cell skeleton-building protein called tubulin (green) marks the tails. When PIP2 levels are too low, some spermatids get mixed up and grow with their heads at the wrong end. Because sperm development is similar across species, studies in fruit flies could help researchers understand male infertility in humans.

Groups of Staphylococcus aureus bacteria (blue) attached to a microstructured titanium surface (green) that mimics an orthopedic implant used in joint replacement. The attachment of pre-formed groups of bacteria may lead to infections because the groups can tolerate antibiotics and evade the immune system. This image was captured using a scanning electron microscope.

More information on the research that produced this image can be found in the Antibiotics paper "Free-floating aggregate and single-cell-initiated biofilms of Staphylococcus aureus" by Gupta et al.

Related to image 6804 and video 6805.

This image represents the structure of TrpRS, a novel member of the tryptophanyl tRNA-synthetase family of enzymes. By helping to link the amino acid tryptophan to a tRNA molecule, TrpRS primes the amino acid for use in protein synthesis. A cluster of iron and sulfur atoms (orange and red spheres) was unexpectedly found in the anti-codon domain, a key part of the molecule, and appears to be critical for the function of the enzyme. TrpRS was discovered in Thermotoga maritima, a rod-shaped bacterium that flourishes in high temperatures.

Stereo triplet of a sea urchin embryo stained to reveal actin filaments (orange) and microtubules (blue). This image is part of a series of images: image 1048, image 1049, image 1050, image 1051 and image 1052.

A protein called tubulin (green) accumulates in the center of a nucleus (outlined in pink) from an aging cell. Normally, this protein is kept out of the nucleus with the help of gatekeepers known as nuclear pore complexes. But NIGMS-funded researchers found that wear and tear to long-lived components of the complexes eventually lowers the gatekeepers' guard. As a result, cytoplasmic proteins like tubulin gain entry to the nucleus while proteins normally confined to the nucleus seep out. The work suggests that finding ways to stop the leakage could slow the cellular aging process and possibly lead to new therapies for age-related diseases.

A zebrafish head with blood vessels shown in purple. Researchers often study zebrafish because they share many genes with humans, grow and reproduce quickly, and have see-through eggs and embryos, which make it easy to study early stages of development.

This image was captured using a light sheet microscope.

Related to video 6933.

Three-dimensional image of misfolded proteins (green) within mitochondria (red). Related to image 5878. Learn more in this press release by The American Association for the Advancement of Science.

The cone cell of the eye allows you to see in color. Appears in the NIGMS booklet Inside the Cell.

The proteasome is a critical multiprotein complex in the cell that breaks down and recycles proteins that have become damaged or are no longer needed. This illustration shows a protein substrate (red) that is bound through its ubiquitin chain (blue) to one of the ubiquitin receptors of the proteasome (Rpn10, yellow). The substrate's flexible engagement region gets engaged by the AAA+ motor of the proteasome (cyan), which initiates mechanical pulling, unfolding and movement of the protein into the proteasome's interior for cleavage into small shorter protein pieces called peptides. During movement of the substrate, its ubiquitin modification gets cleaved off by the deubiquitinase Rpn11 (green), which sits directly above the entrance to the AAA+ motor pore and acts as a gatekeeper to ensure efficient ubiquitin removal, a prerequisite for fast protein breakdown by the 26S proteasome. Related to video 3764.

T cells are white blood cells that are important in defending the body against bacteria, viruses and other pathogens. Each T cell carries proteins, called T-cell receptors, on its surface that are activated when they come in contact with an invader. This activation sets in motion a cascade of biochemical changes inside the T cell to mount a defense against the invasion. Scientists have been interested for some time what happens after a T-cell receptor is activated. One obstacle has been to study how this signaling cascade, or pathway, proceeds inside T cells.

In this image, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The image shows two key steps during the signaling process: clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection.

To learn more how researchers assembled this T-cell receptor pathway, see this press release from HHMI's Marine Biological Laboratory Whitman Center. Related to video 3786.

Georgia Tech associate professor Hang Lu holds a microfluidic chip that is part of a system that uses artificial intelligence and cutting-edge image processing to automatically examine large number of nematodes used for genetic research.

The activator cancer cell culture, right, contains a chemical that causes the cells to emit light when in the presence of immune cells.

This Petri dish contains microscopic roundworms called Caenorhabditis elegans. Researchers used these particular worms to study how C. elegans senses the color of light in its environment.

Hydra magnipapillata is an invertebrate animal used as a model organism to study developmental questions, for example the formation of the body axis.

The three neurons (red) visible in this image were derived from human embryonic stem cells. Undifferentiated stem cells are green here. Image and caption information courtesy of the California Institute for Regenerative Medicine.

The image visualizes a part of the yeast molecular interaction network. The lines in the network represent connections among genes (shown as little dots) and different-colored networks indicate subnetworks, for instance, those in specific locations or pathways in the cell. Researchers use gene or protein expression data to build these networks; the network shown here was visualized with a program called Cytoscape. By following changes in the architectures of these networks in response to altered environmental conditions, scientists can home in on those genes that become central "hubs" (highly connected genes), for example, when a cell encounters stress. They can then further investigate the precise role of these genes to uncover how a cell's molecular machinery deals with stress or other factors. Related to images 3732 and 3733.

This animation shows the effect of exposure to hypochlorous acid, which is found in certain types of immune cells, on bacterial proteins. The proteins unfold and stick to one another, leading to cell death.

This is a fibroblast, a connective tissue cell that plays an important role in wound healing. Normal fibroblasts have smooth edges. In contrast, this spiky cell is missing a protein that is necessary for proper construction of the cell's skeleton. Its jagged shape makes it impossible for the cell to move normally. In addition to compromising wound healing, abnormal cell movement can lead to birth defects, faulty immune function, and other health problems.

This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.

Drugs enter different layers of skin via intramuscular, subcutaneous, or transdermal delivery methods. See image 2532 for a labeled version of this illustration. Featured in Medicines By Design.

Like a building supported by a steel frame, a cell contains its own sturdy internal scaffolding made up of proteins, including microtubules. Researchers studying snapshots of microtubules have proposed a model for how these structural elements shorten and lengthen, allowing a cell to move, divide, or change shape. This picture shows an intermediate step in the model: Smaller building blocks called tubulins peel back from the microtubule in thin strips. Knowing the operations of the internal scaffolding will enhance our basic understanding of cellular processes.

Crystals of bovine milk alpha-lactalbumin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

Mycobacterium tuberculosis, the bacterium that causes tuberculosis, has infected one-quarter of the world's population and causes more than one million deaths each year, according to the World Health Organization.

Xenopus laevis, the African clawed frog, has long been used as a model organism for studying embryonic development. The frog embryo on the left lacks the developmental factor Sizzled. A normal embryo is shown on the right.

Microtubules (magenta) and tau protein (light blue) in a cell model of tauopathy. Researchers believe that tauopathy—the aggregation of tau protein—plays a role in Alzheimer’s disease and other neurodegenerative diseases. This image was captured using Stochastic Optical Reconstruction Microscopy (STORM).

Related to images 6889, 6890, and 6891.

Crystals of porcine trypsin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

This image mostly shows normal cultured epithelial cells expressing green fluorescent protein targeted to the Golgi apparatus (yellow-green) and stained for actin (magenta) and DNA (cyan). The middle cell is an abnormal large multinucleated cell. All the cells in this image have a Golgi but not all are expressing the targeted recombinant fluorescent protein.

A light microscope image of a cell from the endosperm of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones. Staining shows microtubules in red and chromosomes in blue. Here, condensed chromosomes are clearly visible and have lined up in the middle of the dividing cell.

Related to images 1010, 1011, 1012, 1013, 1014, 1015, 1016, 1018, 1019, and 1021.

Vibrio fischeri (2 mm in length) is the exclusive symbiotic partner of the Hawaiian bobtail squid, Euprymna scolopes. After this bacterium uses its flagella to swim from the seawater into the light organ of a newly hatched juvenile, it colonizes the host and loses the appendages. This image was taken using a scanning electron microscope.

Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.

To become products, reactants must overcome an energy hill. See image 2525 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

A spore from the bacterium Bacillus subtilis shows four outer layers that protect the cell from harsh environmental conditions.

Speckle microscopy analysis of actin cytoskeleton force. This is an example of NIH-supported research on single-cell analysis. Images in related series; Related to 2799, 2800, 2801, 2802 and 2803.

This image shows a layer of retinal pigment epithelium cells derived from human embryonic stem cells, highlighting the nuclei (red) and cell surfaces (green). This kind of retinal cell is responsible for macular degeneration, the most common cause of blindness. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to image 3286

Cell-like compartments that spontaneously emerged from scrambled frog eggs, with nuclei (blue) from frog sperm. Endoplasmic reticulum (red) and microtubules (green) are also visible. Image created using confocal microscopy.

For more photos of cell-like compartments from frog eggs view: 6584, 6585, 6586, 6591, 6592.

For videos of cell-like compartments from frog eggs view: 6587, 6588, 6589, and 6590.

In this image, recombinant probes known as FingRs (Fibronectin Intrabodies Generated by mRNA display) were expressed in a cortical neuron, where they attached fluorescent proteins to either PSD95 (green) or Gephyrin (red). PSD-95 is a marker for synaptic strength at excitatory postsynaptic sites, and Gephyrin plays a similar role at inhibitory postsynaptic sites. Thus, using FingRs it is possible to obtain a map of synaptic connections onto a particular neuron in a living cell in real time.

The structure of the pore-forming protein VDAC-1 from humans. This molecule mediates the flow of products needed for metabolism--in particular the export of ATP--across the outer membrane of mitochondria, the power plants for eukaryotic cells. VDAC-1 is involved in metabolism and the self-destruction of cells--two biological processes central to health.

Related to images 2491, 2495, and 2488.

A light organ (~0.5 mm across) of a Hawaiian bobtail squid, Euprymna scolopes, stained blue. At the time of this image, the crypts within the tissues of only one side of the organ had been colonized by green-fluorescent protein-labeled Vibrio fischeri cells, which can be seen here in green. This image was taken using confocal fluorescence microscopy.

Related to images 7016, 7017, 7018, and 7019.

What looks a little like distant planets with some mysterious surface features are actually assemblies of proteins normally found in the cell's nucleolus, a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that makes proteins from messenger RNAs.

However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.

This photo of nucleolus proteins in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows each of the nucleolus compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue). The researchers have found that these compartments spontaneously fuse with each other on encounter without mixing with the other compartments.

For more details on this research, see this press release from Princeton. Related to video 3789, video 3791 and image 3793.

From PDB entry 3c6k, Crystal structure of human spermine synthase in complex with spermidine and 5-methylthioadenosine.

Stained cross section of a mouse tail.

Like a group of barnacles hanging onto a rock, these human cells hang onto a matrix coated glass slide. Actin stress fibers, stained magenta, and the protein vinculin, stained green, make this adhesion possible. The fibroblast nuclei are stained blue.

In this video, Rice University scientists used molecular modeling with a mathematical algorithm called AWSEM (for associative memory, water-mediated, structure and energy model) and structural data to analyze how a transcription factor called nuclear factor kappa B (NFkB) is removed from DNA to stop gene activation. AWSEM uses the interacting energies of their components to predict how proteins fold. At the start, the NFkB dimer (green and yellow, in the center) grips DNA (red, to the left), which activates the transcription of genes. IkB (blue, to the right), an inhibitor protein, stops transcription when it binds to NFkB and forces the dimer to twist and release its hold on DNA. The yellow domain at the bottom of IkB is the PEST domain, which binds first to NFkB. For more details about this mechanism called molecular stripping, see here.