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Enzymes convert subtrates into products (with labels)
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Enzymes convert substrates into products very quickly. See image 2521 for an unlabeled version of this illustration. Featured in The Chemistry of Health. Crabtree + Company View MediaIntracellular forces
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Force vectors computed from actin cytoskeleton flow. This is an example of NIH-supported research on single-cell analysis. Gaudenz Danuser, Harvard Medical School View MediaTiny strands of tubulin, a protein in a cell's skeleton
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Just as our bodies rely on bones for structural support, our cells rely on a cellular skeleton. Pakorn Kanchanawong, National University of Singapore and National Heart, Lung, and Blood Institute, National Institutes of Health; and Clare Waterman, National Heart, Lung, and Blood Institute, National Institutes of Health View MediaCysteine dioxygenase from mouse
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Model of the mammalian iron enzyme cysteine dioxygenase from a mouse. Center for Eukaryotic Structural Genomics, PSI View MediaGroup of fluorescent C. elegans showing muscle and ribosomal protein
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Three C. elegans, tiny roundworms, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. Jarod Rollins, Mount Desert Island Biological Laboratory. View MediaTrp_RS - tryptophanyl tRNA-synthetase family of enzymes
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This image represents the structure of TrpRS, a novel member of the tryptophanyl tRNA-synthetase family of enzymes. View MediaDrosophila (fruit fly) myosin 1D motility assay
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Actin gliding powered by myosin 1D. Note the counterclockwise motion of the gliding actin filaments. Serapion Pyrpassopoulos and E. Michael Ostap, University of Pennsylvania View MediaCCP enzyme
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The enzyme CCP is found in the mitochondria of baker’s yeast. Scientists study the chemical reactions that CCP triggers, which involve a water molecule, iron, and oxygen. Protein Data Bank. View MediaSeeing signaling protein activation in cells 01
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Cdc42, a member of the Rho family of small guanosine triphosphatase (GTPase) proteins, regulates multiple cell functions, including motility, proliferation, apoptosis, and cell morphology. Klaus Hahn, University of North Carolina, Chapel Hill Medical School View MediaDNA replication origin recognition complex (ORC)
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A study published in March 2012 used cryo-electron microscopy to determine the structure of the DNA replication origin recognition complex (ORC), a semi-circular, protein complex (yellow) that recogni Huilin Li, Brookhaven National Laboratory View MediaHsp33 figure 1
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Featured in the March 15, 2012 issue of Biomedical Beat. Related to Hsp33 Figure 2, image 3355. Ursula Jakob and Dana Reichmann, University of Michigan View MediaA molecular switch strips transcription factor from DNA
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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 Davit Potoyan and Peter Wolynes View MediaStetten Lecture 2017poster image
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This image is featured on the poster for Dr. Rommie Amaro's 2017 Stetten Lecture. Dr. Rommie Amaro, University of California, San Diego View MediaZika virus
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Zika virus is shown in cross section at center left. On the outside, it includes envelope protein (red) and membrane protein (magenta) embedded in a lipid membrane (light purple). Amy Wu and Christine Zardecki, RCSB Protein Data Bank. View MediaFluorescent C. elegans showing muscle and ribosomal protein
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C. elegans, a tiny roundworm, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. Jarod Rollins, Mount Desert Island Biological Laboratory. View MediaBeta-galactosidase montage showing cryo-EM improvement--transparent background
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Composite image of beta-galactosidase showing how cryo-EM’s resolution has improved dramatically in recent years. Older images to the left, more recent to the right. Veronica Falconieri, Sriram Subramaniam Lab, National Cancer Institute View MediaBuilding blocks and folding of proteins
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Proteins are made of amino acids hooked end-to-end like beads on a necklace. To become active, proteins must twist and fold into their final, or "native," conformation. Crabtree + Company View MediaWorm sperm
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To develop a system for studying cell motility in unnatrual conditions -- a microscope slide instead of the body -- Tom Roberts and Katsuya Shimabukuro at Florida State University disassembled and rec Tom Roberts, Florida State University View MediaRepairing DNA
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Like a watch wrapped around a wrist, a special enzyme encircles the double helix to repair a broken strand of DNA. Tom Ellenberger, Washington University School of Medicine View MediaMovie of the 19S proteasome subunit processing a protein substrate
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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. Andreas Martin, HHMI View MediaMeasles virus proteins
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A cross section of the measles virus in which six proteins (enlarged on the outside of the virus) work together to infect cells. Amy Wu and Christine Zardecki, RCSB Protein Data Bank. View MediaMolecular interactions
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This network map shows molecular interactions (yellow) associated with a congenital condition that causes heart arrhythmias and the targets for drugs that alter these interactions (red and blue). Ravi Iyengar, Mount Sinai School of Medicine View MediaStructure of Glutamate Dehydrogenase
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Some children are born with a mutation in a regulatory site on this enzyme that causes them to over-secrete insulin when they consume protein. Judy Coyle, Donald Danforth Plant Science Center View MediaCellular aging
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A protein called tubulin (green) accumulates in the center of a nucleus (outlined in pink) from an aging cell. Maximiliano D'Angelo and Martin Hetzer, Salk Institute View MediaCytoskeleton
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The three fibers of the cytoskeleton--microtubules in blue, intermediate filaments in red, and actin in green--play countless roles in the cell. Judith Stoffer View MediaRNA folding in action
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An RNA molecule dynamically refolds itself as it is being synthesized. When the RNA is short, it ties itself into a “knot” (dark purple). Julius Lucks, Northwestern University View MediaMolecules blocking Huntington's protein production
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The molecules that glow blue in these cultured cells prevent the expression of the mutant proteins that cause Huntington's disease. Jiaxin Hu, David W. Dodd and Robert H. E. Hudson, UT Southwestern Medical Center View MediaBrains of sleep-deprived and well-rested fruit flies
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On top, the brain of a sleep-deprived fly glows orange because of Bruchpilot, a communication protein between brain cells. These bright orange brain areas are associated with learning. Chiara Cirelli, University of Wisconsin-Madison View MediaSerum albumin structure 1
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Serum albumin (SA) is the most abundant protein in the blood plasma of mammals. SA has a characteristic heart-shape structure and is a highly versatile protein. Wladek Minor, University of Virginia View MediaBiosensors illustration
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A rendering of an activity biosensor image overlaid with a cell-centered frame of reference used for image analysis of signal transduction. Gaudenz Danuser, Harvard Medical School View MediaCryo-electron tomography of a Caulobacter bacterium
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3D image of Caulobacter bacterium with various components highlighted: cell membranes (red and blue), protein shell (green), protein factories known as ribosomes (yellow), and storage granules Peter Dahlberg, Stanford University. View MediaDense tubular matrices in the peripheral endoplasmic reticulum (ER) 1
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Superresolution microscopy work on endoplasmic reticulum (ER) in the peripheral areas of the cell showing details of the structure and arrangement in a complex web of tubes. Jennifer Lippincott-Schwartz, Howard Hughes Medical Institute Janelia Research Campus, Virginia View MediaDynamic cryo-EM model of the human transcription preinitiation complex
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Gene transcription is a process by which information encoded in DNA is transcribed into RNA. Eva Nogales, Berkeley Lab View MediaRNase A (1)
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A crystal of RNase A protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures. Alex McPherson, University of California, Irvine View MediaProtein crystals
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Structural biologists create crystals of proteins, shown here, as a first step in a process called X-ray crystallography, which can reveal detailed, three-dimensional protein structures. Alex McPherson, University of California, Irvine View MediaBlood clots show their flex
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Blood clots stop bleeding, but they also can cause heart attacks and strokes. Eric Lee, University of Illinois at Urbana-Champaign View MediaBeta-galactosidase montage showing cryo-EM improvement--gradient background
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Composite image of beta-galactosidase showing how cryo-EM’s resolution has improved dramatically in recent years. Older images to the left, more recent to the right. Veronica Falconieri, Sriram Subramaniam Lab, National Cancer Institute View MediaCrane fly spermatocyte undergoing meiosis
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A crane fly spermatocyte during metaphase of meiosis-I, a step in the production of sperm. Michael Shribak, Marine Biological Laboratory/University of Chicago. View MediaNucleosome
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Like a strand of white pearls, DNA wraps around an assembly of special proteins called histones (colored) to form the nucleosome, a structure responsible for regulating genes and condensing DNA strand Karolin Luger, Colorado State University View MediaZ rings in bacterial division
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Lab-made liposomes contract where Z rings have gathered together and the constriction forces are greatest (arrows). Masaki Osawa, Duke University View MediaVDAC-1 (4)
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The structure of the pore-forming protein VDAC-1 from humans. Gerhard Wagner, Harvard Medical School View MediaPlastic-eating enzymes
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PETase enzyme degrades polyester plastic (polyethylene terephthalate, or PET) into monohydroxyethyl terephthalate (MHET). Amy Wu and Christine Zardecki, RCSB Protein Data Bank. View Media3D image of actin in a cell
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Actin is an essential protein in a cell's skeleton (cytoskeleton). It forms a dense network of thin filaments in the cell. Xiaowei Zhuang, Howard Hughes Medical Institute, Harvard University View MediaMeasles virus
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A cross section of the measles virus in which six proteins work together to infect cells. The measles virus is extremely infectious; 9 out of 10 people exposed will contract the disease. Amy Wu and Christine Zardecki, RCSB Protein Data Bank. View MediaA2A adenosine receptor
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The receptor is shown bound to an inverse agonist, ZM241385. Raymond Stevens, The Scripps Research Institute View MediaMicrotubule dynamics in real time
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Cytoplasmic linker protein (CLIP)-170 is a microtubule plus-end-tracking protein that regulates microtubule dynamics and links microtubule ends to different intracellular structures. Gary Borisy, Marine Biology Laboratory View MediaAntitoxin GhoS (Illustration 1)
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Structure of the bacterial antitoxin protein GhoS. GhoS inhibits the production of a bacterial toxin, GhoT, which can contribute to antibiotic resistance. Rebecca Page and Wolfgang Peti, Brown University and Thomas K. Wood, Pennsylvania State University View MediaRNA Polymerase II
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NIGMS-funded researchers led by Roger Kornberg solved the structure of RNA polymerase II. David Bushnell, Ken Westover and Roger Kornberg, Stanford University View MediaDisease-susceptible Arabidopsis leaf
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This is a magnified view of an Arabidopsis thaliana leaf after several days of infection with the pathogen Hyaloperonospora arabidopsidis. Jeff Dangl, University of North Carolina, Chapel Hill View MediaDynein moving along microtubules
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Dynein (green) is a motor protein that “walks” along microtubules (red, part of the cytoskeleton) and carries its cargo along with it. This video was captured through fluorescence microscopy. Morgan DeSantis, University of Michigan. View Media