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Resources
NIH RePORTER
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Dashboard of TWD Funded Programs
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Workforce Developement
Related Information
Contact Information
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Resources
Enhancing Diversity in Training Programs
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Laboratory Safety and Guidelines
Training Resources
Capacity Building
Division for Research Capacity Building
Institutional Development Award (IDeA)
Native American Research Centers for Health (NARCH)
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
NIGMS Funding Policies
Which Research Grant Is Right for Me?
How to Apply
Grant Application and Review Process
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
NIH RePORTER
Research Using Human Subjects or Specimens
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STEM Teaching Resources
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Image & Video Gallery
NIGMS-Supported Resources
Protein Alphabet
Other Resources
Biomedical Beat Blog
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News
News from NIGMS
NIGMS in the News
COVID-19 News
Biomedical Beat Blog
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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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2342
308
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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2748
559
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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2343
309
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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2337
112
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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2339
114
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
Featured as the June 2007 Protein
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Initiative
Structure
of the Month
Molecular
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2345
310
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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3487
664
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
BK_Virtual_
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2340
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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181
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
structures
should serve as a valuable resource for biomedical research
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6601
904
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
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structure
of HIV capsid_thumbnail Thumbnail 12 KB 12/10/2020
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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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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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2365
183
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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2372
117
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
10/29/2020 4:26:44 PM
Type Name Media Type File Size Modified
Chosen as the December 2007 Protein
Structure
Initiative
Structure
of the Month
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2355
246
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
structure
prediction methods
The
structure
consists of identical protein subunits, each shown in a different color
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2367
184
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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3720
817
This wreath represents the molecular structure of a protein, Cas4, which is part of a system, known as CRISPR, that bacteria use to protect themselves against viral invaders. The green ribbons show the protein's structure, and the red balls show the location of iron and sulfur molecules important for the protein's function. Scientists harnessed Cas9, a different protein in the bacterial CRISPR system, to create a gene-editing tool known as CRISPR-Cas9. Using this tool, researchers are able to study a range of cellular processes and human diseases more easily, cheaply and precisely. In December, 2015, Science magazine recognized the CRISPR-Cas9 gene-editing tool as the "breakthrough of the year." Read more about Cas4 in the December 2015 Biomedical Beat post <a href="https://biobeat.nigms.nih.gov/2015/12/cool-images-a-holiday-themed-collection/">A Holiday-Themed Image Collection</a>.
12/3/2020 8:52:01 PM
12/3/2020 8:52:01 PM
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Cas4 nuclease protein
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3307
445
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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3597
739
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. Related to video <a href=http://images.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3307><i>3307</i></a> that 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."
10/8/2024 1:27:54 PM
10/8/2024 1:27:54 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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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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Novel biosensor system maps the timing and location of Rac protein activation in a living mouse embryo fibroblast.
8/20/2020 6:22:04 PM
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Structure
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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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Solution NMR structure of protein target WR41 (left) from <i>C. elegans</i>. Noting the unanticipated structural similarity to the ubiquitin protein (Ub) found in all eukaryotic cells, researchers discovered that WR41 is a Ub-like modifier, ubiquitin-fold modifier 1 (Ufm1), on a newly uncovered ubiquitin-like pathway. Subsequently, the PSI group also determined the three-dimensional structure of protein target HR41 (right) from humans, the E2 ligase for Ufm1, using both NMR and X-ray crystallography.
10/29/2020 4:56:46 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
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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
Molecular
Structures
drug development, model, protein
structure
string;#<DIV><img style='max-width:100px;max-height
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Molecular model of the struture of heme. Heme is a small, flat molecule with an iron ion (dark red) at its center. Heme is an essential component of hemoglobin, the protein in blood that carries oxygen throughout our bodies. This image first appeared in the <a href="http://publications.nigms.nih.gov/findings/sept13/hooked-on-heme.asp">September 2013 issue of Findings Magazine</a>.
9/27/2020 4:35:34 AM
9/27/2020 4:35:34 AM
Type Name Media Type File Size Modified
Structure
of heme, top view
Hi Sharon, The two heme
structures
can be made public
Molecular
Structures
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The TRPA1 protein is responsible for the burn you feel when you taste a bite of sushi topped with wasabi. Known therefore informally as the "wasabi receptor," this protein forms pores in the membranes of nerve cells that sense tastes or odors. Pungent chemicals like wasabi or mustard oil cause the pores to open, which then triggers a tingling or burn on our tongue. This receptor also produces feelings of pain in response to chemicals produced within our own bodies when our tissues are damaged or inflamed. Researchers used cryo-EM to reveal the structure of the wasabi receptor at a resolution of about 4 angstroms (a credit card is about 8 million angstroms thick). This detailed structure can help scientists understand both how we feel pain and how we can limit it by developing therapies to block the receptor. For more on 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>.
12/17/2020 5:41:39 PM
12/17/2020 5:41:39 PM
Type Name Media Type File Size Modified
Researchers used cryo-EM to reveal the structure of the wasabi receptor at a
an image of the TRPA1 ion channel
structure
that you describe in your 2015 Nature paper
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Lab-made liposomes contract where Z rings have gathered together and the constriction forces are greatest (arrows). The top picture shows a liposome, and the bottom picture shows fluorescence from Z rings (arrows) inside the same liposome simultaneously.
8/20/2020 5:58:21 PM
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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. Without molecules that can mend such breaks, cells can malfunction, die, or become cancerous. Related to image <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=131">2330</a>.
9/9/2020 2:16:07 AM
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Ribosomes are complex machines made up of more than 50 proteins and three or four strands of genetic material called ribosomal RNA (rRNA). The busy cellular machines make proteins, which are critical to almost every structure and function in the cell. To do so, they read following protein-building instructions, which come as strands of messenger RNA. Ribosomes are found in all forms of cellular life—people, plants, animals, even bacteria. This illustration of a bacterial ribosome was produced using detailed information about the position of every atom in the complex. Several antibiotic medicines work by disrupting bacterial ribosomes but leaving human ribosomes alone. Scientists are carefully comparing human and bacterial ribosomes to spot differences between the two. Structures that are present only in the bacterial version could serve as targets for new antibiotic medications.
12/18/2020 8:00:42 PM
12/18/2020 8:00:42 PM
Structures
that are present only in the bacterial version could serve as targets for new
make proteins, which are critical to almost every
structure
and function in the cell
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A protein called kinesin (blue) is in charge of moving cargo around inside cells and helping them divide. It's powered by biological fuel called ATP (bright yellow) as it scoots along tube-like cellular tracks called microtubules (gray).
9/8/2020 11:21:32 PM
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A crystal of RNase A protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
8/6/2020 6:44:52 PM
8/6/2020 6:44:52 PM
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Model based on X-ray crystallography of the structure of a small heat shock protein complex from the bacteria, <i>Methanococcus jannaschii</i>. <i>Methanococcus jannaschii</i> is an organism that lives at near boiling temperature, and this protein complex helps it cope with the stress of high temperature. Similar complexes are produced in human cells when they are "stressed" by events such as burns, heart attacks, or strokes. The complexes help cells recover from the stressful event.
10/29/2020 4:52:21 PM
10/29/2020 4:52:21 PM
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Model of a human protein associated with the adenylyl cyclase, an enzyme involved in intracellular signaling.
10/29/2020 3:00:19 PM
10/29/2020 3:00:19 PM
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Structure of sortase b from the bacterium <i>B. anthracis</i>, which causes anthrax. Sortase b is an enzyme used to rob red blood cells of iron, which the bacteria need to survive.
10/29/2020 4:53:35 PM
10/29/2020 4:53:35 PM
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A 3D model of the human endoplasmic reticulum membrane protein complex (EMC) that identifies its nine essential subunits. The EMC plays an important role in making membrane proteins, which are essential for all cellular processes. This is the first atomic-level depiction of the EMC. Its structure was obtained using single-particle cryo-electron microscopy.
12/6/2021 8:02:51 PM
12/6/2021 8:02:51 PM
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Model of a major secreted protein of unknown function, which is only found in mycobacteria, the class of bacteria that causes tuberculosis. Based on structural similarity, this protein may be involved in host-bacterial interactions.
10/29/2020 4:43:06 PM
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A three-dimensional representation of the structure of E2, a key antigen protein involved with Hepatitis C Virus infection.
11/1/2021 2:32:51 PM
11/1/2021 2:32:51 PM
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A crystal of Bence Jones protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
8/6/2020 4:03:59 PM
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NIGMS-funded researchers led by Roger Kornberg solved the structure of RNA polymerase II. This is the enzyme in mammalian cells that catalyzes the transcription of DNA into messenger RNA, the molecule that in turn dictates the order of amino acids in proteins. For his work on the mechanisms of mammalian transcription, Kornberg received the Nobel Prize in Chemistry in 2006.
9/18/2020 5:05:13 PM
9/18/2020 5:05:13 PM
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The feeding tube, or pharynx, of a planarian worm with cilia shown in red and muscle fibers shown in green
10/19/2020 6:12:17 AM
10/19/2020 6:12:17 AM
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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. Appears in the NIGMS booklet <a href="http://publications.nigms.nih.gov/insidethecell/" target="_blank"><i>Inside the Cell</i></a>.
10/28/2020 4:14:44 PM
10/28/2020 4:14:44 PM
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High-resolution time lapse of epithelial (skin) cell migration and wound healing. It shows an image taken every 13 seconds over the course of almost 14 minutes. The images were captured with quantitative orientation-independent differential interference contrast (DIC) microscope (left) and a conventional DIC microscope (right). <Br><Br>More information about the research that produced this video can be found in the <em>Journal of Microscopy</em> paper <a href="https://onlinelibrary.wiley.com/doi/10.1111/jmi.12682/">“An Orientation-Independent DIC Microscope Allows High Resolution Imaging of Epithelial Cell Migration and Wound Healing in a Cnidarian Model”</a> by Malamy and Shribak.
6/30/2022 4:45:48 PM
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This image shows the structure of synapse, or junction between two nerve cells in three-dimensions. From the brain of a mouse.
12/18/2020 9:53:12 PM
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An image of the area of the mouse brain that serves as the 'master clock,' which houses the brain's time-keeping neurons. The nuclei of the clock cells are shown in blue. A small molecule called VIP, shown in green, enables neurons in the central clock in the mammalian brain to synchronize. More information about the research behind this image can be found in a <a href="http://biobeat.nigms.nih.gov/">Biomedical Beat Blog</a> posting from November 2013.
5/13/2022 12:40:18 PM
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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
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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 strands to fit into the cell's nucleus. Researchers once thought that nucleosomes regulated gene activity through their histone tails (dotted lines), but a 2010 study revealed that the structures' core also plays a role. The finding sheds light on how gene expression is regulated and how abnormal gene regulation can lead to cancer. Featured in the May 19, 2010, issue of <a href=http://publications.nigms.nih.gov/biobeat/10-05-19/index.html#1 target="_blank"><em>Biomedical Beat</em></a>.
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to form the nucleosome, a
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The HIV capsid is pear-shaped structure that is made of proteins the virus needs to mature and become infective. The capsid is inside the virus and delivers the virus' genetic information into a human cell. To better understand how the HIV capsid does this feat, scientists have used computer programs to simulate its assembly. This image shows a series of snapshots of the steps that grow the HIV capsid. A model of a complete capsid is shown on the far right of the image for comparison; the green, blue and red colors indicate different configurations of the capsid protein that make up the capsid “shell.” The bar in the left corner represents a length of 20 nanometers, which is less than a tenth the size of the smallest bacterium. Computer models like this also may be used to reconstruct the assembly of the capsids of other important viruses, such as Ebola or the Zika virus. <br><br> The studies reporting this research were published in <a href="http://www.nature.com/ncomms/2016/160513/ncomms11568/full/ncomms11568.html"><i>Nature Communications</i></a> and <a href="http://www.nature.com/nature/journal/v469/n7330/full/nature09640.html"><i>Nature</i></a>. <br><br> To learn more about how researchers used computer simulations to track the assembly of the HIV capsid, see <a href=" https://news.uchicago.edu/article/2016/06/14/simulations-describe-hivs-diabolical-delivery-device">this press release from the University of Chicago</a>.
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Ribbon diagram showing the structure of Ribonuclease P with tRNA.
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Ribonuclease_P High 468 KB 6/3/2016 3:38 PM aamishral2 (NIH/NIGMS) [C
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