|
|
|
|
|
|
WEHI-TV DNA Molecular Animation
|
|
Select an animation from the table below
|
|
|
|
Drew Berry has been developing innovative techniques for representing the science of bio-medical discovery since 1995.
His specialisation in science is founded upon post-graduate honours (BSc Hons) and Masters of Science (MSc) degrees in cell biology from the University of Melbourne, where he conducted research on the structure and behaviour of living cells. His science background is instrumental for his interaction with scientists and his grasp of the complex bio-medical subjects he portrays.
A unique feature of his animations is the scientific accuracy imbued during their design and creation. Each of his animations is founded on the latest scientific data sets, such as X-ray crystallography, so that details such as molecular shapes, sizes and real-time dynamics are as accurate as possible. During the production of the DNA animations, many eminent scientists, including several Nobel Laureates, reviewed and critiqued the animations during their development. The exceptional effort applied to ensuring scientific accuracy will give the animations the longevity and confidence required for their high-profile roles.
An equally important characteristic of Drew Berry's animations is the quality of imagery and their visually engaging design. Over a number of years, Drew Berry has developed novel techniques from the sophisticated digital tools used for special effects in Hollywood feature films. For the DNA animations, Drew Berry had to invent a suite of new techniques to solve the particular challenges of these molecular subjects. The level of technical sophistication of the DNA animations has not been achieved before, and it is expected that they will remain as the very best available for many years to come.
To contact Drew, email wehi-tv@wehi.edu.au
Various basic animations of DNA. These animations were originally designed for the opening ceremony performance of the 2003 International Congress of Genetics (http://www.geneticscongress2003.com).
The DNA model was developed from the X-ray crystallographic structure available from the Protein Data Bank (http://www.rcsb.org/pdb/). The DNA's jiggle was added to suggest Brownian motion caused by thermal energy and agitation by surrounding molecules. The jiggle was driven by a fractal-based dynamics system created with Maya (http://www.alias.com) animation software.
This animation demonstrates the structure of DNA by unwinding then unzipping the double helix.
Various basic animations of DNA. These animations were originally designed for the opening ceremony performance of th
e 2003 International Congress of Genetics (http://www.geneticscongress2003.com).
The DNA model was developed from the X-ray crystallographic structure available from the Protein Data Bank (http://www.rcsb.org/pdb/
). The DNA's jiggle was added to suggest Brownian motion caused by thermal energy and agitation by surrounding molecules. The jiggle
was driven by a fractal-based dynamics system created with Maya (http://www.alias.com) animation software.
This animation is a medium shot of DNA strands.
Various basic animations of DNA. These animations were originally designed for the opening ceremony performance of th
e 2003 International Congress of Genetics (http://www.geneticscongress2003.com).
The DNA model was developed from the X-ray crystallographic structure available from the Protein Data Bank (http://www.rcsb.org/pdb/
). The DNA's jiggle was added to suggest Brownian motion caused by thermal energy and agitation by surrounding molecules. The jiggle
was driven by a fractal-based dynamics system created with Maya (http://www.alias.com) animation software.
A close-up of the DNA molecule, created with a shallow depth-of-field camera for visual interest.
This animation presents the various levels of DNA organization
(wrapping) within mitotic chromosomes. Although the histone, nucleosome and
chromatin structures were derived from published data, the middle "levels" of
wrapping depicted here are controversial as to what form they take or even
whether they exist. The top-level coils that create the chromatids in this
animation are not usually shown in text-book diagrams, yet published data
presents good evidence for their existence and structure as it is presented
here.
The histone, nucleosome and DNA models were derived from
their PDB (http://www.rcsb.org/pdb/ )
structures and other published data. The histone's N-terminal arms were added
by hand, as they are not resolved by X-ray crystallography, due to their
highly dynamic nature. The time-lapse footage of the mitotic cell was filmed
by Prof Jeremy Pickett-Heaps (http://www.cytographics.com/).
Transcription factors assemble at a DNA promoter
region found at the start of a gene. Promoter regions are characterised
by the DNA's base sequence, which contains the repetition TATATA \311 and
for this reason is known as the "TATA box".
The TATA box is gripped by the transcription factor
TFIID (yellow-brown) that marks the attachment point for RNA polymerase
and associated transcription factors. In the middle of TFIID is the
TATA Binding Protein subunit, which recognises and fastens onto the
TATA box. It's tight grip makes the DNA kink 90\373, which is thought
to serve as a physical landmark for the start of a gene.
A mediator (purple) protein complex arrives carrying
the enzyme RNA polymerase II (blue-green). It manoeuvres the RNA
polymerase into place. Other transcription factors arrive (TFIIA
and TFIIB - small blue molecules) and lock into place. Then TFIIH
(green) arrives. One of its jobs is to pry apart the two strands
of DNA (via helicase action) to allow the RNA polymerase to get access
to the DNA bases.
Finally, the initiation complex requires contact
with activator proteins, which bind to specific sequences of DNA
known as enhancer regions. These regions can be thousands of base
pairs away from the initiation complex. The consequent bending of
the activator protein/enhancer region into contact with the initiation-complex
resembles a scorpion's tail in this animation.
The activator protein triggers the release of the
RNA polymerase, which runs along the DNA transcribing the gene into
mRNA (yellow ribbon).
Transcription factors assemble at a DNA promoter
region found at the start of a gene. Promoter regions are characterised
by the DNA's base sequence, which contains the repetition TATATA \311 and
for this reason is known as the "TATA box".
The TATA box is gripped by the transcription factor
TFIID (yellow-brown) that marks the attachment point for RNA polymerase
and associated transcription factors. In the middle of TFIID is the
TATA Binding Protein subunit, which recognises and fastens onto the
TATA box. It's tight grip makes the DNA kink 90\373, which is thought
to serve as a physical landmark for the start of a gene.
A mediator (purple) protein complex arrives carrying
the enzyme RNA polymerase II (blue-green). It manoeuvres the RNA
polymerase into place. Other transcription factors arrive (TFIIA
and TFIIB - small blue molecules) and lock into place. Then TFIIH
(green) arrives. One of its jobs is to pry apart the two strands
of DNA (via helicase action) to allow the RNA polymerase to get access
to the DNA bases.
Finally, the initiation complex requires contact
with activator proteins, which bind to specific sequences of DNA
known as enhancer regions. These regions can be thousands of base
pairs away from the initiation complex. The consequent bending of
the activator protein/enhancer region into contact with the initiation-complex
resembles a scorpion's tail in this animation.
The activator protein triggers the release of the
RNA polymerase, which runs along the DNA transcribing the gene into
mRNA (yellow ribbon).
The DNA Project was initiated as a trans-national effort comprising
a formidable team of people and organizations including James Watson,
the Howard Hughes Medical Institute, Alfred P. Sloan Foundation,
Cold Spring Harbour Lab, GlaxoSmithKline, Channel 4 Television (UK),
PBS (USA), The University of North Carolina at Chapel Hill, the Red,
Green and Blue Company, and Windfall Films.
The molecular dynamics and shapes in these animations
were based on X-ray crystallographic models and other published scientific
data sets. Many eminent scientists, including several Nobel Laureates,
critiqued the animations during their development. Particular
effort was made to ensure the relative shapes, sizes and 'real-time'
dynamics were as accurate as possible. The primary software used
for building the animations was Maya ( http://www.alias.com).
The animator, Drew Berry, had the key responsibility of translating
DNA molecular science into accurate and engaging visual explanations.
Drew created a comprehensive suite of animations that covers essential
DNA science topics such as DNA replication, the "central dogma" of
molecular biology (DNA makes RNA makes Protein), and current biotechnology
techniques.
The outcomes of the DNA Project include:
- "DNA", a major five-episode documentary series, screening on
ABC-TV (Australia), PBS (USA), Channel 4 (UK), with other countries
worldwide to be confirmed. "DNA" is the definitive account
of how the human race found the secret of life as told by the
scientists
who made the breakthroughs, with animation visually interpreting
the molecular science that is described.
-
"DNA: The Secret of Life" museum film, a 30 minute film focusing on the
discovery of the DNA double helix, the structure and science
of the molecule, and the future of genomics research. The film's
intended target audience is 12 year olds through to adult, and
will be screened at museums around the world;
- DNAi.org, the DNA
education web portal, providing interactive DNA science learning
resources to teachers and students, including
downloadable versions of the animations, a 3D guided tour of
the genomic landscape, and provocative interviews with eminent
scientists and Nobel Laureates; and
- The "DNA" DVD designed for classroom
exploration, containing a comprehensive selection of the animations,
interviews and other
materials from the DNA Project.
The first shot in this animation is of a Transcription
Initiation Complex, as described in Part
1: Transcription Initiation Complex
The RNA polymerase unzips a small portion of the
DNA helix exposing the bases on each strand. One of the strands acts
as a template for the synthesis of an RNA molecule. The base-sequence
code is transcribed by matching these DNA bases with RNA subunits,
forming a long RNA polymer chain.
This type of RNA is called messenger RNA (mRNA).
The job of mRNA is to carry the message from the DNA to a ribosome,
for translation of the gene into protein.
The final step in protein synthesis occurs in a
complex catalytic machine called the ribosome. This ultramicroscopic
machine assembles three-dimensional protein molecules that are essential
for us to live.
The message in mRNA (yellow) is decoded inside the
ribosome (purple and light blue) and translated into a chain of amino
acids (red).
The ribosome is composed of one large (purple) and
one small subunit (light blue), each with a specific task to perform.
The small subunit's task is to match the triple letter code, known
as a codon, to the anticodon at the base of each tRNA (green). The
large subunit's task is to link the amino acids together into a chain.
The amino acid chain exits the ribosome through a tunnel in the large
subunit, then folds up into a three-dimensional protein molecule.
As the mRNA is ratcheted through the ribosome, the
mRNA sequence is translated into an amino acid sequence. The sequence
of mRNA condons determines the specific amino acids that are added
to the growing polypeptide chain. Selection of the correct amino
acid is determined by complimentary base pairing between the mRNA's
codon and the tRNA's anticodon. The codons are shown in this animation
during the close up of the mRNA entering the ribosome. The codons
are indicated as triplet groups of yellow-brown bases.
tRNA (green) is a courier molecule carrying a single
amino acid (red tip) as its parcel.
During the amino acid chain synthesis, the tRNA
steps through three locations inside the ribosome, referred to as
the A-site, P-site and E-site. tRNA enters the ribosome and
lodges in the A-site, where it is tested for a correct codon-anticodon
match. If the tRNA's anticondon correctly matches the mRNA condon,
it is stepped through to the P-site by a conformational change in
the ribosome. In the P-site the amino acid carried by the tRNA is
attached to the growing end of the amino acid chain.
The addition of amino acids is a three step cycle
- The tRNA enters the ribosome at the A-site and is tested for
a codon-anticodon match with the mRNA.
- If it is a correct match, the tRNA is shifted to the P-site
and the amino acid it carries is added to the end of the peptide
chain. The mRNA is also ratcheted three nucleotides (1 codon).
- The spent tRNA is moved to the E-site and then ejected from
the ribosome.
A typical eukaryotic cell contains millions of ribosomes
in its cytoplasm.
Many details, such as elongation factors (eg EFTu),
have been omitted from this animation. This animation represents
an idealised system with no incorrect tRNAs entering the ribosome,
and consequently no error correction at the A-site.
This animation depicts the process of DNA recombination
using the restriction enzyme EcoRI.
The animation opens with a view of a DNA plasmid
loop. An EcoRI enzyme approaches and attaches to the DNA's major
groove. The enzyme then runs along the groove scanning the DNA for
the base sequence xGAATTCx. When it finds this sequence it breaks
the sugar-phosphate bonds on either side of DNA, splicing the plasmid.
A gene (glowing DNA) with complementary 'sticky ends" then attaches
to the end of the plasmid. The enzyme DNA Ligase (looking like frozen
peas in this animation) then repairs the nicks in the sugar-phosphate
backbone, joining the two DNA strands.
This animation depicts aspects of the haemoglobin
molecules and the mutant form that causes the disease sickle cell
anaemia.
Red blood cells supply oxygen to the body using
their cargo of haemoglobin, a protein that can capture and release
oxygen. In this animation a haemoglobin molecule first assemble from
subunits. The haemoglobin binds with four molecules of oxygen (blue)
in the lungs, and then releases them again when the blood passes
through body tissues with low oxygen concentrations.
When the sickle-mutant haemoglobin gives up it's
oxygen to the tissues, a conformational change results in an amino
acid (yellow-green) to pop out and cause the molecule to stick together
and form stiff fibers. These long fibers distort red blood cells
into their characteristic "sickle" shape (not shown). The sickle
red blood cells can then clog small blood vessels, depriving vital
organs of oxygen, resulting in anaemia, jaundice, organ damage and
other symptoms.
|
|
All media and images contained on this site are
© Copyright 2008 The Walter & Eliza Hall Institute.
For further information, contact
the Webmaster or contact WEHI-TV
Back to WEHI-TV
|
|