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Institutional Development Award (IDeA)
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Science Education Partnership Awards (SEPA)
Support of Competitive Research (SCORE)
Related Information
DRCB News
DRCB Staff Contacts
Resources
NIH RePORTER
Grants and Funding
Funding Opportunities
Current NIGMS Funding Opportunities
Parent Announcements for Investigator-Initiated Applications
Research Funding
Research Project Grants (NIH Parent R01)
Research With Activities Related to Diversity (ReWARD)
Maximizing Investigators' Research Awards (MIRA)
Instrumentation Grant Program for Resource-Limited Institutions (RLI-S10)
Undergraduate-Focused Institutions
Small Business Research
Multidisciplinary Teams/Collaborative Research
Technology Development
Research Resources
Clinical Studies and Trials
Conferences and Scientific Meetings
Administrative Supplements
All Funding Opportunities
Grant Application and Post-Award Information
Which Research Grant Is Right for Me?
How to Apply
Grant Application and Review Process
NIGMS Funding Policies
Post-Award Information
Talking to NIH Staff About Your Application and Grant
Considerations for Multiple Principal Investigator (MPI) Applications
Resources
Attribution of NIH/NIGMS Support
Message to NIGMS Investigators
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Research Using Human Subjects or Specimens
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STEM Teaching Resources
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Image & Video Gallery
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Protein Alphabet
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3438
593
The chemical structure of the morphine molecule
8/22/2020 4:44:39 PM
8/22/2020 4:44:39 PM
Morphine_
structure
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Crystal structure of the beta2-adrenergic receptor protein. This is the first known structure of a human G protein-coupled receptor, a large family of proteins that control critical bodily functions and the action of about half of today's pharmaceuticals. Featured as one of the November 2007 Protein Structure Initiative Structures of the Month.
10/29/2020 2:35:50 PM
10/29/2020 2:35:50 PM
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NMR solution structure of a plant protein that may function in host defense. This protein was expressed in a convenient and efficient wheat germ cell-free system. Featured as the June 2007 Protein Structure Initiative Structure of the Month.
10/29/2020 2:40:04 PM
10/29/2020 2:40:04 PM
Type Name Media Type File Size Modified
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Initiative
Structure
of the Month
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X-ray structure of a new DNA repair enzyme superfamily representative from the human gastrointestinal bacterium <i>Enterococcus faecalis</i>. European scientists used this structure to generate homologous structures. Featured as the May 2007 Protein Structure Initiative Structure of the Month.
10/29/2020 2:46:36 PM
10/29/2020 2:46:36 PM
European scientists used this
structure
to generate homologous
structures
Featured as the May 2007 Protein
Structure
Initiative
Structure
of the Month
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The goal of the PSI is to determine the three-dimensional shapes of a wide range of proteins by solving the structures of representative members of each protein family found in nature. The collection of structures should serve as a valuable resource for biomedical research scientists.
10/29/2020 4:12:18 PM
10/29/2020 4:12:18 PM
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The collection of
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should serve as a valuable resource for biomedical research
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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 recognizes and binds DNA to start the replication process. The ORC appears to wrap around and bend approximately 70 base pairs of double stranded DNA (red and blue). Also shown is the protein Cdc6 (green), which is also involved in the initiation of DNA replication. The video shows the structure from different angles. From a Brookhaven National Laboratory <a href=http://www.bnl.gov/bnlweb/pubaf/pr/PR_display.asp?prID=1391&template=Today target="_blank">news release</a>, "Study Reveals How Protein Machinery Binds and Wraps DNA to Start Replication." See related image <a href=http://images.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3597><i>3597</i></a>.
12/22/2020 11:01:10 PM
12/22/2020 11:01:10 PM
The light brown shading represents the
structure
obtained by cryo-EM
The ribbon diagram
structures
came from X-ray crystallography and were superimposed on the cryo-EM
structure
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This animation shows atoms of the HIV capsid, the shell that encloses the virus's genetic material. Scientists determined the exact structure of the capsid using a variety of imaging techniques and analyses. They then entered this data into a supercomputer to produce this image. Related to image <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=3477">3477</a>.
11/14/2023 1:23:27 PM
11/14/2023 1:23:27 PM
Atomic-Level
Structure
of the HIV Capsid High 20229 KB 12/10/2020 5:41 PM
atomic-level
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This crystal structure shows a conserved hypothetical protein from <i>Mycobacterium tuberculosis</i>. Only 12 other proteins share its sequence homology, and none has a known function. This structure indicates the protein may play a role in metabolic pathways. Featured as one of the August 2007 Protein Structure Initiative Structures of the Month.
10/29/2020 2:48:36 PM
10/29/2020 2:48:36 PM
This
structure
indicates the protein may play a role in metabolic pathways
Featured as one of the August 2007 Protein
Structure
Initiative
Structures
of the Month
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115
This is the first structure of a protein derived from the metagenomic sequences collected during the Sorcerer II Global Ocean Sampling project. The crystal structure shows a barrel protein with a ferredoxin-like fold and a long chain fatty acid in a deep cleft (shaded red). Featured as one of the August 2007 Protein Structure Initiative Structures of the Month.
10/29/2020 2:41:27 PM
10/29/2020 2:41:27 PM
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This ribbon drawing of a protein hand drawn and colored by researcher Jane Richardson in 1981 helped originate the ribbon representation of proteins that is now ubiquitous in molecular graphics. The drawing shows the 3-dimensional structure of the protein triose phosphate isomerase. The green arrows represent the barrel of eight beta strands in this structure and the brown spirals show the protein's eight alpha helices. A black and white version of this drawing originally illustrated a <a href=http://kinemage.biochem.duke.edu/teaching/anatax target="_blank">review article</a> in <i>Advances in Protein Chemistry</i>, volume 34, titled "Anatomy and Taxonomy of Protein Structures." The illustration was selected as Picture of The Day on the English Wikipedia for November 19, 2009. Other important and beautiful images of protein structures by Jane Richardson are available in her <a href=http://commons.wikimedia.org/wiki/User:Dcrjsr/gallery_of_protein_structure target="_blank">Wikimedia gallery</a>.
8/18/2020 7:55:11 PM
8/18/2020 7:55:11 PM
The drawing shows the 3-dimensional
structure
of the protein triose phosphate isomerase
barrel of eight beta strands in this
structure
and the brown spirals show the protein's
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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." A protein's final shape enables it to accomplish its function. Featured in <a href=http://publications.nigms.nih.gov/structlife/ target="_blank"><i>The Structures of Life</i></a>.
5/13/2024 6:21:12 PM
5/13/2024 6:21:12 PM
/education/Booklets/The-Structures-of-Life/Pages/Home.aspx"><em>The
Structures
of Life</em
The
Structures
of Life page 3
Molecular
Structures
structure
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Model of a member from the Tex protein family, which is implicated in transcriptional regulation and highly conserved in eukaryotes and prokaryotes. The structure shows significant homology to a human transcription elongation factor that may regulate multiple steps in mRNA synthesis.
10/29/2020 2:37:40 PM
10/29/2020 2:37:40 PM
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A special "messy" region of a potassium ion channel is important in its function.
9/8/2020 10:55:58 PM
9/8/2020 10:55:58 PM
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2561
544
Histone proteins loop together with double-stranded DNA to form a structure that resembles beads on a string. See image 2560 for an unlabeled version of this illustration. Featured in <a href=http://publications.nigms.nih.gov/thenewgenetics/ target="_blank"><i>The New Genetics</i></a>.
10/23/2020 7:26:47 PM
10/23/2020 7:26:47 PM
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Model of a protein, antigen 85B, that is the most abundant protein exported by <i>Mycobacterium tuberculosis</i>, 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.
10/29/2020 4:41:39 PM
10/29/2020 4:41:39 PM
Type Name Media Type File Size Modified
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A global "map of the protein structure universe." The Berkeley Structural Genomics Center has developed a method to visualize the vast universe of protein structures in which proteins of similar structure are located close together and those of different structures far away in the space. This map, constructed using about 500 of the most common protein folds, reveals a highly non-uniform distribution, and shows segregation between four elongated regions corresponding to four different protein classes (shown in four different colors). Such a representation reveals a high-level of organization of the protein structure universe.
10/29/2020 4:16:23 PM
10/29/2020 4:16:23 PM
a representation reveals a high-level of organization of the protein
structure
universe
Map of protein
structures
01
Molecular
Structures
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A model of thymidylate synthase complementing protein from <i>Thermotoga maritime</i>.
10/29/2020 4:55:29 PM
10/29/2020 4:55:29 PM
Type Name Media Type File Size Modified
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2373
118
Crystal structure of oligoendopeptidase F, a protein slicing enzyme from <i>Bacillus stearothermophilus</i>, a bacterium that can cause food products to spoil. The crystal was formed using a microfluidic capillary, a device that enables scientists to independently control the parameters for protein crystal nucleation and growth. Featured as one of the July 2007 Protein Structure Initiative Structures of the Month.
10/29/2020 4:30:39 PM
10/29/2020 4:30:39 PM
Type Name Media Type File Size Modified
Technologies Center for Gene to 3D
Structure
/Midwest Center for Structural Genomics
Molecular
Structures
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Catalases are some of the most efficient enzymes found in cells. Each catalase molecule can decompose millions of hydrogen peroxide molecules every second—working as an antioxidant to protect cells from the dangerous form of reactive oxygen. Different cells build different types of catalases. The human catalase that protects our red blood cells, shown on the left from PDB entry <a href="https://www.rcsb.org/structure/1QQW">1QQW</a>, is composed of four identical subunits and uses a heme/iron group to perform the reaction. Many bacteria scavenge hydrogen peroxide with a larger catalase, shown in the center from PDB entry <a href="https://www.rcsb.org/structure/1IPH">1IPH</a>, that uses a similar arrangement of iron and heme. Other bacteria protect themselves with an entirely different catalase that uses manganese ions instead of heme, as shown at the right from PDB entry <a href="https://www.rcsb.org/structure/1JKU">1JKU</a>.
2/5/2024 2:17:16 PM
2/5/2024 2:17:16 PM
as shown at the right from PDB entry <a href="https://www.rcsb.org/
structure
/1JKU">1JKU</a
Molecular
Structures
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3314
448
Opioid receptors on the surfaces of brain cells are involved in pleasure, pain, addiction, depression, psychosis, and other conditions. The receptors bind to both innate opioids and drugs ranging from hospital anesthetics to opium. Researchers at The Scripps Research Institute, supported by the NIGMS Protein Structure Initiative, determined the first three-dimensional structure of a human opioid receptor, a kappa-opioid receptor. In this illustration, the submicroscopic receptor structure is shown while bound to an agonist (or activator). The structure is superimposed on a poppy flower, the source of opium. From a Scripps Research Institute <a href=http://www.scripps.edu/news/press/20120321stevens.html target="_blank">news release</a>.
12/23/2020 4:46:54 PM
12/23/2020 4:46:54 PM
by the NIGMS Protein
Structure
Initiative, determined the first three-dimensional
structure
of a human opioid receptor, a
Human opioid receptor
structure
superimposed on poppy
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Histone proteins loop together with double-stranded DNA to form a structure that resembles beads on a string. See image 2561 for a labeled version of this illustration. Featured in <a href=http://publications.nigms.nih.gov/thenewgenetics/ target="_blank"><i>The New Genetics</i></a>.
10/23/2020 7:26:17 PM
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HIV is a retrovirus, a type of virus that carries its genetic material not as DNA but as RNA. Long before anyone had heard of HIV, researchers in labs all over the world studied retroviruses, tracing out their life cycle and identifying the key proteins the viruses use to infect cells. When HIV was identified as a retrovirus, these studies gave AIDS researchers an immediate jump-start. The previously identified viral proteins became initial drug targets. See images <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=2514">2514</a> and <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=2515">2515</a> for labeled versions of this illustration. Featured in <a href=http://publications.nigms.nih.gov/structlife/ target="_blank"><i>The Structures of Life</i></a>.
9/25/2020 4:26:31 PM
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X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Found in the journal, Nature, Chemical Biology 8, 366-374 (2012). Part of an image series: <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3413">image 3413</a> , <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3414">image 3414</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3415">image 3415</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3416">image 3416</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3417">image 3417</a> and <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3418">image 3418</a>.
12/23/2020 11:13:50 PM
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A crystal of porcine trypsin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
8/6/2020 7:45:47 PM
8/6/2020 7:45:47 PM
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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. GhoS is the first known bacterial antitoxin that works by cleaving the messenger RNA that carries the instructions for making the toxin. More information can be found in the paper: Wang X, Lord DM, Cheng HY, Osbourne DO, Hong SH, Sanchez-Torres V, Quiroga C, Zheng K, Herrmann T, Peti W, Benedik MJ, Page R, Wood TK. <a href="http://www.ncbi.nlm.nih.gov/pubmed/22941047" target="_blank">A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS</a>. Nat Chem Biol. 2012 Oct;8(10):855-61. Related to <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3427">image 3427</a>.
8/22/2020 4:31:28 PM
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Crystals of porcine alpha amylase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
8/6/2020 7:43:47 PM
8/6/2020 7:43:47 PM
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X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Found in the journal, Nature, Chemical Biology 8, 366-374 (2012). Series of seven images. Related to <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3413">image 3413</a> , <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3415">image 3415</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3416">image 3416</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3417">image 3417</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3418">image 3418</a> and <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3419">image 3419</a>.
12/23/2020 11:04:41 PM
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Crystals of fungal lipase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
8/6/2020 7:42:01 PM
8/6/2020 7:42:01 PM
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Living primary mouse embryonic fibroblasts. Mitochondria (green) stained with the mitochondrial membrane potential indicator, rhodamine 123. Nuclei (blue) are stained with DAPI. Caption from a November 26, 2012 <a href= "http://www.uphs.upenn.edu/news/News_Releases/2012/11/energy/">news release </a> from U Penn (Penn Medicine).
8/22/2020 6:35:39 PM
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From: Kevin Foskett [mailto:foskett@mail.med.upenn.edu] Sent: Wednesday, May 15, 2013 11:14 AM To: Kreeger, Karen Subject: Re: Permission from NIGMS
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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). Featured in the May 19, 2010, issue of <a href=http://publications.nigms.nih.gov/biobeat/10-05-19/index.html#4 target="_blank"><em>Biomedical Beat</em></a>.
8/18/2020 7:18:39 PM
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Model of the enzyme aminopeptidase N from the human pathogen <i>Neisseria meningitidis</i>, which can cause meningitis epidemics. The structure provides insight on the active site of this important molecule.
10/29/2020 2:43:00 PM
10/29/2020 2:43:00 PM
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Model of the enzyme Nicotinic acid phosphoribosyltransferase. This enzyme, from the archaebacterium, <i>Pyrococcus furiosus</i>, is expected to be structurally similar to a clinically important human protein called B-cell colony enhancing factor based on amino acid sequence similarities and structure prediction methods. The structure consists of identical protein subunits, each shown in a different color, arranged in a ring.
10/29/2020 3:44:23 PM
10/29/2020 3:44:23 PM
factor based on amino acid sequence similarities and
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prediction methods
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Structure of a magnesium transporter protein from an antibiotic-resistant bacterium (<i>Enterococcus faecalis</i>) found in the human gut. Featured as one of the June 2007 Protein Sructure Initiative Structures of the Month.
10/29/2020 2:58:36 PM
10/29/2020 2:58:36 PM
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This image shows how the CRISPR surveillance complex is disabled by two copies of anti-CRISPR protein AcrF1 (red) and one AcrF2 (light green). These anti-CRISPRs block access to the CRISPR RNA (green tube) preventing the surveillance complex from scanning and targeting invading viral DNA for destruction.
12/21/2020 5:09:58 PM
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Crystal structure of a protein with unknown function from <i>Xanthomonas campestris</i>, a plant pathogen. Eight copies of the protein crystallized to form a ring. Chosen as the December 2007 Protein Structure Initiative Structure of the Month.
10/29/2020 4:26:44 PM
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Chosen as the December 2007 Protein
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An NMR solution structure model of the transfer RNA splicing enzyme endonuclease in humans (subunit Sen15). This represents the first structure of a eukaryotic tRNA splicing endonuclease subunit.
10/29/2020 3:06:53 PM
10/29/2020 3:06:53 PM
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A global "map of the protein structure universe" indicating the positions of specific proteins. The preponderance of small, less-structured proteins near the origin, with the more highly structured, large proteins towards the ends of the axes, may suggest the evolution of protein structures.
10/29/2020 4:18:37 PM
10/29/2020 4:18:37 PM
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The G switch allows our bodies to respond rapidly to hormones. G proteins act like relay batons to pass messages from circulating hormones into cells. A hormone (red) encounters a receptor (blue) in the membrane of a cell. Next, a G protein (green) becomes activated and makes contact with the receptor to which the hormone is attached. Finally, the G protein passes the hormone's message to the cell by switching on a cell enzyme (purple) that triggers a response. See image 2536 and 2538 for other versions of this image. Featured in <a href=http://publications.nigms.nih.gov/medbydesign/ target="_blank"><i>Medicines By Design</i></a>.
10/9/2020 4:46:41 PM
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Scientists have long known that multicellular organisms use biological molecules produced by one cell and sensed by another to transmit messages that, for instance, guide proper development of organs and tissues. But it's been a puzzle as to how molecules dumped out into the fluid-filled spaces between cells can precisely home in on their targets.<br> Using living tissue from fruit flies, a team led by Thomas Kornberg of the University of California, San Francisco, has shown that typical cells in animals can talk to each other via long, thin cell extensions called cytonemes (Latin for "cell threads") that may span the length of 50 or 100 cells. The point of contact between a cytoneme and its target cell acts as a communications bridge between the two cells.<br> More information about the research behind this image can be found in a <a href="http://biobeat.nigms.nih.gov/2014/02/animal-cells-reach-out-and-touch-to-communicate/" target=_blank>Biomedical Beat </a>Blog posting from February 2014.
10/5/2020 5:54:08 AM
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A knotted protein from an archaebacterium called <i>Methanobacterium thermoautotrophicam</i>. This organism breaks down waste products and produces methane gas. Protein folding theory previously held that forming a knot was beyond the ability of a protein, but this structure, determined at Argonne's Structural Biology Center, proves differently. Researchers theorize that this knot stabilizes the amino acid subunits of the protein.
10/29/2020 4:32:27 PM
10/29/2020 4:32:27 PM
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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 bouquets 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.
8/23/2023 2:01:13 PM
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fertility,
structure
, Grant 2R01GM062276
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Dengue virus is a mosquito-borne illness that infects millions of people in the tropics and subtropics each year. Like many viruses, dengue is enclosed by a protective membrane. The proteins that span this membrane play an important role in the life cycle of the virus. Scientists used cryo-EM to determine the structure of a dengue virus at a 3.5-angstrom resolution to reveal how the membrane proteins undergo major structural changes as the virus matures and infects a host. The image shows a side view of the structure of a protein composed of two smaller proteins, called E and M. Each E and M contributes two molecules to the overall protein structure (called a heterotetramer), which is important for assembling and holding together the viral membrane, i.e., the shell that surrounds the genetic material of the dengue virus. The dengue protein's structure has revealed some portions in the protein that might be good targets for developing medications that could be used to combat dengue virus infections. To learn more about cryo-EM, see the blog post <a href="https://biobeat.nigms.nih.gov/2016/02/cryo-electron-microscopy-reveals-molecules-in-ever-greater-detail/">Cryo-Electron Microscopy Reveals Molecules in Ever Greater Detail.</a> For a video of the entire virus rotating, see <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3748"> video 3748</a>, and for a still image of the virus, see <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3756">image 3756</a>.
12/17/2020 6:24:54 PM
12/17/2020 6:24:54 PM
The image shows a side view of the
structure
of a protein composed of two smaller proteins
about the video of the dengue virus
structure
you had determined by cryo-EM and which is
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Ribbon diagram showing the structure of Ribonuclease P with tRNA.
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A 3D reconstruction of a transient receptor potential channel called TRPV5 that was created based on cryo-electron microscopy images. TRPV5 is primarily found in kidney cells and is essential for reabsorbing calcium into the blood.
8/10/2020 11:36:21 PM
8/10/2020 11:36:21 PM
Currently, her laboratory is using cryo-EM to determine TRPV5 channel
structures
in conditions that better mimic those found in the body, including the presence
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Model of an enzyme, PanC, that is involved in the last step of vitamin B5 biosynthesis in <i>Mycobacterium tuberculosis</i>. PanC is essential for the growth of <i>M. tuberculosis</i>, which causes most cases of tuberculosis, and is therefore a potential drug target.
10/29/2020 4:48:43 PM
10/29/2020 4:48:43 PM
Type Name Media Type File Size Modified
hi_Rv3602c_M Medium 106 KB 6/3/2016 3:10 PM
Molecular
Structures
protein
structure
, drug development
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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.
5/20/2024 1:55:04 PM
5/20/2024 1:55:04 PM
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TIRF_motility_movie (2) High 18389 KB 5/22/2024 2:19 PM aamershaha (NIH/NIGMS) [C
It was acquired in my lab here at the
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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. In order to fulfill these diverse roles, the timing and location of Cdc42 activation must be tightly controlled. Klaus Hahn and his research group use special dyes designed to report protein conformational changes and interactions, here in living neutrophil cells. Warmer colors in this image indicate higher levels of activation. Cdc42 looks to be activated at cell protrusions.
5/9/2022 1:34:32 PM
5/9/2022 1:34:32 PM
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whole_cell_2 High 611 KB 6/3/2016 3:11 PM aamishral2 (NIH/NIGMS) [C
Warmer colors in this image indicate
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Under the microscope, an <i>E. coli</i> cell lights up like a fireball. Each bright dot marks a surface protein that tells the bacteria to move toward or away from nearby food and toxins. Using a new imaging technique, researchers can map the proteins one at a time and combine them into a single image. This lets them study patterns within and among protein clusters in bacterial cells, which don't have nuclei or organelles like plant and animal cells. Seeing how the proteins arrange themselves should help researchers better understand how cell signaling works. A movie containing this image was featured in the August 19, 2009, issue of <a href=http://publications.nigms.nih.gov/biobeat/09-08-19/index.html#1 target="_blank"><em>Biomedical Beat</em></a>.
8/28/2020 5:59:20 PM
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A growing Vibrio cholerae (cholera) biofilm. Cholera bacteria form colonies called biofilms that enable them to resist antibiotic therapy within the body and other challenges to their growth. <br></br>Each slightly curved comma shape represents an individual bacterium from assembled confocal microscopy images. Different colors show each bacterium’s position in the biofilm in relation to the surface on which the film is growing.
3/3/2021 5:54:14 PM
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Jing_Bassler_biofilm High 133 KB 3/3/2021 12:52 PM Walter, Taylor (NIH/NIGMS) [C
Please let me know if you
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Model of an enzyme, PanB, from <i>Mycobacterium tuberculosis</i>, the bacterium that causes most cases of tuberculosis. This enzyme is an attractive drug target.
10/29/2020 4:44:22 PM
10/29/2020 4:44:22 PM
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hi_Rv2225_L Low 53 KB 6/3/2016 3:10 PM aamishral2 (NIH/NIGMS) [C
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