Am. J. Trop. Med. Hyg., 83(1), 2010, pp. 1–6
Copyright © 2010 by The American Society of Tropical Medicine and Hygiene
Thank you indeed to Christopher Plowe for the very gener-
ous introduction—I think it was perhaps too generous. Chris
showed the list of fellows and students who have worked with
me at National Institutes of Health (NIH), and great credit
really goes to them. I have been fortunate and privileged to
have been surrounded by the brilliance of all of these individ-
uals and their accomplishments through the years. Also, Chris
did not name himself in the photographs with our Malian col-
leagues, instead referring to himself only as one of the “less
talented” fellows. Not at all! In fact, Chris was overly generous
to me when he spoke of our field work in Mali on chloroquine
resistance. It really was Chris’ project with Abdoulaye Djimdé
while I was collaborating on much of that work. So I return
the credit for that to Chris, with the comment that it was par-
ticularly rewarding to see the impact on health in the villages
where we collaborated with our Malian colleagues to deliver
relatively inexpensive medicines that worked wonders.
Tonight marks the end of a wonderful experience for me
as your ASTMH President. The period has left me with last-
ing memories, new colleagues, and friends. And it is a great
satisfaction to say that this extraordinary Society continues
to grow in strength and collective voice as the leading inter-
national organization of scientists and clinicians dedicated to
tropical medicine and global health. ASTMH is alive with an
abundance of positive spirit and teamwork in our membership.
This year we have held our largest and most successful Annual
Meeting ever, with over 3,400 registrants. We have also seen
excellent progress in areas of membership, policy and advo-
cacy, media communications, and awards program funding.
Time does not allow me to thank by name everyone who made
this progress possible. However, I would like to express my
gratitude to some individuals in particular:
To Sally Finney, our Executive Director, for her initia-
tive and careful attention to our ASTMH activities this
year. These have included the Policy and Advocacy work
with Kent Campbell, the upcoming ASTMH Constitution
and Bylaws revisions, the launch of our Public Relations
Committee, the media relations contract with the MWW
Group, and the coordination of our Executive Committee
and Council meetings;
To Judy DeAcetis, Lyn Maddox, Matthew Lesh, and their
Sherwood Group Colleagues for their attentive care to this
year’s operations including the meeting arrangements, the
drive to boost membership, and the wide-ranging adminis-
trative needs of our Society.
To Chris King and the approximately 100 members of our
Scientific Program Committee for their contributions of
time, thought, and effort putting together a terrific Meeting
Agenda this year.
To the members of the
ASTMH Council, especially Josh
Berman, Peter Weller, Jim Kazura, Ed Ryan, Claire Panosian,
Joe Vinetz, Steve Higgs, plus so many other Society mem-
bers I have not named—thank you all for your generous ser-
vice to ASTMH this year.
Finally, to my wife Marilyn, daughter Dianne, and sons Alex
and Nick and their wives Lauren and Alysen: your love and
unaffected eloquence in our family have meant everything
to me over the years; and thank you very much for your sup-
port through a busy and eventful 2009.
Formative influences. The call to give this Society’s
presidential address presents an opportunity to choose among
almost limitless topics across subjects of tropical public health,
scientific discovery, our history, and aspects of policy and
advocacy tied to the goals of ASTMH . As an attendee of these
addresses in previous years, I have enjoyed hearing previous
presidents talk of their career experiences in the context of
their ASTMH interests, particularly when these have touched
on major events that have molded and restructured our
perspective and activities in today’s world. My thoughts in
this regard returned me to some memories from my graduate
student experiences at the University of Chicago. These were
under two of my PhD advisors in structural biology, Robert
Josephs and Paul B. Sigler. My thesis work in those years was
on the fibers and crystals of deoxygenated hemoglobin that
can form in erythrocytes when there is a mutation from valine
to glutamate in the sixth position of the hemoglobin beta
chain, namely, the sickle-cell mutation. 1, 2 Those experiences
were among the stimuli that eventually brought me to malaria
research, a personal path that I will not go into tonight. Instead,
I would like to use this address to touch upon some of the
profound influences of the scientist who more than any other
established the field of my PhD research. He determined
the structure of hemoglobin, investigated the effects of its
mutations, and established core legacies of molecular medicine
and molecular biology at the Cavendish Laboratory and
Cambridge University in England.
A long-term quest of fundamental discovery. Max Perutz
decided to pursue the structure of hemoglobin in 1937, at
a time when genes were generally thought to be proteins,
and when proteins acting as enzymes had only recently
been recognized to catalyze chemical reactions in living
systems. Perutz saw protein structure as a central problem of
biology, and he recognized that the only way to approach it
was by x-ray crystallography. 3 He also saw hemoglobin as a
molecule of immense importance and mystery, especially in
the mechanisms by which it transported oxygen and carbon
dioxide in the bloodstream. The existence of regular crystals
of hemoglobin suggested to Perutz that the molecule’s
enormous number of atoms could take a specific shape and
that the resulting structure would hold the key to how the
Optimism, Persistence, and Our Collective Crystal Ball
Thomas E. Wellems *
Member, American Society of Tropical Medicine and Hygiene
*Address correspondence to Thomas E. Wellems, c/o Administrative
Director, ASTMH Headquarters, 111 Deer Lake Road, Suite 100,
The Sherwood Group, Deerfield, IL 60015. E-mail: thomas.wellems@
molecule worked. However, in 1937, no one knew how to go
about solving the structure of such a protein; indeed, there was
widespread belief that the prospects for success were bleak
and the goal was scarcely realistic, if not unattainable. 4, 5 Perutz,
under generous support and advice from William Lawrence
Bragg and John Desmond Bernal, 6 nevertheless pursued the
My first exposure to the optimism and persistence with
which Max Perutz took on the hemoglobin problem was in
my reading of a paper he contributed in 1948 in honor of the
British physiologist Sir Joseph Barcroft. At that point his goal
must have seemed distant indeed, for he wrote:
“On the face of it … an attempt to analyze the crystal
structure of hemoglobin, or of any crystalline protein for
that matter, looks about as promising as a journey to the
This at a time when space travel was still a story of science
fiction and the dream of reaching the moon was only the stuff
of a love song. It was a marvel, I thought, to read Perutz’s
assessment of the hemoglobin structure problem as a possibly
forlorn undertaking. He had no clear route yet to the protein
structure—in fact, his model at that time would prove wrong—
but he concluded in his paper that there remained “a variety
of different ways of approach to the problem of protein struc-
ture. Some of these ways have proved dead ends, but many are
still leading on.” 7 His decades of single-minded pursuit of a
distant goal of major importance, by paths not at all clear, not
even sure to be possible, struck me as a tremendous model for
a career in scientific discovery.
Perutz received critical support for his work during this
period from the Medical Research Council and its Secretary
Sir Edward Mellanby. In 1947, Bragg met with Mellanby and
explained the difficulty of the work, the remote chances of suc-
cess and, if success were achieved, the likelihood that it might
well be a long time before the information would be of practi-
cal use to medicine. Mellanby accepted the risk, and he decided
to support the research. 4 After Mellanby retired in 1949, Sir
Harold Himsworth became Secretary of the MRC and con-
tinued strong support for the work. Eventually, Perutz wrote
a book in 1992 entitled Protein Structure: New Approaches to
Disease and Therapy , and he dedicated it to Himsworth, writ-
ing that “[Himsworth’s] foresight and courage led him to sup-
port my colleagues and my early work on protein structures
when there was only the faintest hope of it ever benefitting
By 1970, a year after the Apollo 11 moon landing, Perutz’s
determination was not only vindicated by his solution of the
structure of hemoglobin ( Figure 1 )—he had also developed
an essential description of the cooperative operations by
which it functions as a breathing molecule. 9 The exchange of
gases and the physiological phenomenon of the Bohr effect
were explained at the level of individual atoms, and he and
Hermann Lehmann had linked clinical manifestations of a
variety of genetic mutations to the positions and influence of
individual amino acid substitutions. 10
The breakthroughs of Perutz and his colleagues in crystal-
lography not only revealed the hemoglobin molecule in all
its wonder and, as he put it, its “simple beauty” 5 —the break-
throughs also set the stage for the elucidation of a world of
structures from biological systems. More than 50,000 protein
structures are now available over the internet from the RCSB
Protein Data Bank, 11 and applications have reached into vital
areas of medicine including, for example, the development of
drugs against influenza, protease inhibitors against HIV-1/
AIDS, and captopril for the treatment of hypertension and
heart failure. 12
Yet Perutz’s legacy extends even more broadly. As group
head of the Cavendish Laboratory Unit under Medical
Research Council (MRC) support, and subsequently as
Chairman of the Cambridge MRC Laboratory of Molecular
Biology, Perutz recruited and supported an astonishing num-
ber of brilliant colleagues.
It is still fascinating to recall the names and accomplishments
from the Cavendish Unit and the Cambridge Laboratory:
Watson and Crick and the DNA double helix; John Kendrew
and the structure of myoglobin; Sydney Brenner and the
Caenorhabditis elegans animal development model; Vernon
Ingram and identification of the β6 hemoglobin substitution
responsible for sickle-cell anemia; Hugh Huxley and the slid-
ing filament model for muscle contraction; Cesar Milstein and
the hybridoma technique for monoclonal antibody produc-
tion; Aaron Klug and the structural determination of nucleic
acid-protein complexes; and Frederick Sanger and sequencing
methods that elucidated the first full DNA sequence of a viral
genome (Phage Φ-X174). 6, 13
Perutz’s belief in enlisting ambitious and creative scientists
and giving them what they needed to succeed was an essential
character of his chairmanship years. He recognized scientific
creativity, he recognized what could kill it, and he understood
the value of an environment in which young scientists were
given the intellectual freedom to pursue their ideas—of an
environment in which they were not told what to do, but they
had to find out what to do by themselves. 4, 5
Science and applications of science. Perutz was deeply
committed to the importance of scientific thinking and the
value of basic research for a foundation of human betterment
and human purposes. He used his voice as a Nobel Laureate
to advocate for human rights and promote his conviction that
Figure 1. Depiction of the crystal structure of human deoxyhe-
moglobin at 1.74 Å resolution. The Protein Data Bank Data (ID:
2HHB) of Fermi and others 33 were downloaded and displayed using
the RCSB Protein Workshop Viewer ( http://www.rcsb.org/pdb/ ). This
figure appears in color at www.ajtmh.org .
“scientists the world over are united by a common purpose,
ideally to discover Nature’s secrets and put them to use for
human benefit”. 14
It was also in Perutz’s nature to value research done for its
own sake, in his words: to “discover the strange workings of a
wonderful world.” 6
Many of you will probably recognize the book written in
1997 by Donald Stokes, Pasteur’s Quadrant: Basic Science and
Technological Innovation . 15 This book was also mentioned
by Carlos Morel in his Commemorative Fund Lecture at last
year’s ASTMH Annual Meeting in New Orleans. 16 Stokes’
history provides an absorbing treatment of the distinctions
that are frequently drawn between classifications of basic
and applied research, and of how these distinctions have been
incorporated into various institutional policies and govern-
ment funding, particularly in the years since Vannevar Bush’s
1945 report Science—the Endless Frontier . 17 Stokes’ thesis is
that classifications of research in a one-dimensional model
from basic to applied often fail to recognize the full range and
motivation of investigations in science. He offers a diagram
of two-dimensions in which research falls into cells or quad-
rants, depending upon the degree to which scientific efforts
are motivated by the goals of 1) fundamental understanding
and 2) considerations of use.
In Stokes’ diagram ( Figure 2 ), the lower right quadrant
includes the work of the inventor Thomas Edison, who was
famous for his quests for applications alone, without inter-
est to develop fundamental scientific theories. The physics
of Niels Bohr is placed in the upper left quadrant because of
his passion for fundamental understanding on the basic level.
And, in the upper right quadrant, are bodies of scientific work
motivated both by curiosity about fundamental principles of
nature and by the search for useful applications. Stokes named
this quadrant after Louis Pasteur, who strove to understand
the processes of disease at the most fundamental level, while
at the same time he worked to develop ways to deal with major
problems including anthrax, milk and wine spoilage, chicken
cholera, rabies, and silk worm infections.
But I wonder how clearly motivations based on “consider-
ations of use” distinguish the quadrants of Pasteur and Bohr.
Pasteur once famously remarked “Il n’existe pas de sciences
appliquées, mais seulement des applications de la science.
[There are no such things as applied sciences, only applica-
tions of science],” 18 also, that science and its applications are
“liées entre elles comme le fruit à l’arbre qui l’a porté [linked
together as fruit is to the tree that has borne it].” 19
With these words in mind, consider Niels Bohr. He was a
profound scientist, a preeminent creator of fundamental phys-
ics and a philosopher of natural phenomena, but he was like-
wise an orchestrator of experimental science, a builder of a
renowned research Institute in Copenhagen, a helper of ref-
ugees, and a passionate advocate for international openness
in the spirit of glastnost. 20 The son of Danish physiologist
Christian Bohr, for whom the Bohr hemoglobin effect studied
by Max Perutz is named, Niels Bohr also looked for ways to
bring physics into biology and medicine. This he did astonish-
ingly well following a 1933 decision by Warren Weaver and the
Rockefeller Foundation to focus on support for experimental
biology as its primary field of interest in the natural sciences.
With funding from the Rockefeller Foundation, Bohr sup-
ported his friend and colleague George de Hevesy, who pur-
sued work with inducible radioactive tracers in Copenhagen
after these were first produced by Marie Curie’s daughter
Irène and her husband Frédéric Joliot. 20 Hevesy’s work with
artificial tracers spurred revolutionary applications in biology
and founded the field of nuclear medicine. 20, 21
Bohr’s enthusiasm for bringing physics to biology had a
notable influence in another direction as well. This was an
influence I first learned about in 1984, shortly after I joined
NIH’s malaria research group under Louis Miller, in the
Laboratory of Parasitic Diseases directed by Franklin Neva.
It was an exciting time: DNA sequences of the Plasmodium
falciparum circumsporozoite protein (CSP) identified by Ruth
Nussenzweig were being published, 22, 23 and I began a project
with Russell Howard to clone and characterize the sequence
of a malaria parasite gene we termed pfhrp2 . 24 Sequence
information from the CSP gene is used today in the RTS,S
recombinant malaria vaccines; and the sequences of PfHRP2
serve as the basis for a number of the rapid diagnostic tests
that are now widely deployed for the detection of P. falci-
parum infection. In 1984, lambda bacteriophages, plasmids,
and selected Escherichia coli strains were the working clon-
ing systems in these projects. For methods and information we
routinely turned to publications from the Cold Spring Harbor
Laboratory, mainly Molecular Cloning: A Laboratory Manual
published in 1982 by Tom Maniatis, Joe Sambrook, and Edward
So, what was the influence that connects Niels Bohr, molec-
ular biology at Cold Spring Harbor, and the cloning methods
for the genes I mentioned? In a 1932 address entitled “Light
and Life,” Bohr reflected on the principles of complementar-
ity in physics and asked whether analogous principles might
be needed to understand living organisms. 26, 27 Max Delbrück,
an associate of Bohr’s in theoretical physics, was so taken with
Figure 2. Quadrant model of research motivations proposed by
the address that he decided to change the course of his career
from physics to biology. 28, 29
Delbrück turned to biology with the view that a detailed
examination of living systems might uncover paradoxical phe-
nomena similar to those that had confronted physicists in
quantum physics. He did not succeed to find such phenom-
ena, eventually coming to the view that all dynamic systems
of biology are reducible and follow the laws of physics and
chemistry. 30 But his search proved extraordinarily fruitful, as
his ideas spurred fundamental investigations into the physical
properties of the gene, and he and Salvador Luria opened up
a new world of molecular genetics in their demonstrations of
evolution by random mutation. Along with Luria, Delbrück
initiated the famous phage group at the Cold Spring Harbor
Laboratory ( www.cshl.edu/history/Delbrück.html ), in the
same spirit of scientific associations that were present in the
Copenhagen group around Bohr. 3
Past is prologue. A half century after the molecular and
genetic breakthroughs of Perutz and Delbrück, we have
before us today entire genome sequences of pathogens and
hosts, and we also have the understanding and wherewithal to
manipulate the components of these living systems as never
before. The advances we are witnessing in biology and medicine
are just some of the benefits of the physical and social sciences
to the human condition, as they join with advances across
areas of nutrition, water and sanitation, telecommunications,
agriculture, energy production, and transportation, with
remarkable potential to improve health and well-being.
In many countries of the world, the effects of these benefits
are evident in two measures of health and well-being: life expec-
tancy at birth and income per person. Some of you are proba-
bly familiar with the trends analysis of these measures by Hans
Rosling, Professor of International Health at the Karolinska
Institutet and Director of the Gapminder Organization. His
presentations bring global health and economic trends to life.
Figure 3 shows a Gapminder series comparing life expectancy
at birth and income per person from 1827, a year roughly
between the time Edward Jenner began using the cowpox vac-
cine against smallpox and the time John Snow removed the
Broad Street pump handle in his great epidemiological advance
against cholera. From a life expectancy range of 25 to 40 years
in the early 1800s, this expectancy has increased for most coun-
tries, increasing first in the industrialized countries, for exam-
ple in Europe and North America. And life expectancy then
shows great improvements in some other large populations,
for example in India and China, where about 50 years ago life
expectancy began increasing at a rate almost twice as fast as
the earlier rates in Europe and North America. For India and
China the increases in life expectancy began some years before
the increases in prosperity. As Rosling points out for these sta-
tistics, “you get wealthy faster if you’re healthy first.”
There is momentum in these gains, and it is in the right
direction. We know that in many countries of Africa and some
other regions of the world, overall improvements have lagged.
But past is prologue, and the momentum of the gains tells us
we can be confident that better conditions of health will be fol-
lowed by increases in prosperity.
I am proud to say it is on these challenges of health that our
ASTMH membership focuses:
We work as a worldwide organization to prevent and con-
trol infectious and other diseases that disproportionately
afflict the global poor.
Our goals include advancing research on tropical diseases,
fostering international scientific collaborations, promoting
science-based policy, and supporting education and career
Figure 3. Gapminder comparisons of life expectancy at birth vs. income per person in 1827, 1887, 1947, and 2007. Colored circles represent
countries from different regions of the world, and the size of each bubble represents a country’s population. Plots were generated from data and
software at the Gapminder web site: http://www.gapminder.org/. This figure appears in color at www.ajtmh.org .
development of professionals in tropical medicine and
President Obama this year pointed out that “Science is
more essential for our prosperity, our security, our health,
our environment, and our quality of life than it has ever been
before” and “… many of the challenges that science and tech-
nology will help us meet are global in character.” 31 Science is
at the heart of our goals in ASTMH , and the innovations that
follow from investments in science, from fundamental discov-
eries and their applications, will give us vital means to meet
A report recently announced by the National Research
Council’s Board on Life Sciences, “ A New Biology for the 21st
Century, ” 32 opens by asking that we imagine a world where:
there is abundant, healthful food for everyone
the environment is resilient and flourishing
there is sustainable, clean energy
good health is the norm
In calling for a national initiative to address these goals, the
report reaffirms the role of fundamental research endeavors
and recommends that they be met by integrated, interdisci-
plinary efforts across the biological and physical sciences.
These recommendations echo the approaches of Perutz, Bohr,
and their colleagues as they brought concepts of physical sci-
ences and new computational technology to great advances in
biology a half century ago. Scientific discovery and its appli-
cations give us the platform for continued progress that will
improve our collective ability to control disease, improve eco-
nomic production, and nourish and support our world’s pop-
ulations. Even in the face of issues of climate change, global
population burden, environmental depredations, and emerg-
ing disease threats, science and its processes give us capacities
scarcely imaginable just a few decades ago; and future capaci-
ties will come that we can scarcely imagine today.
The ways of thinking that have enabled us to travel to the
moon, and have given us new ways to understand ourselves and
the universe, have the power to meet these goals. But we must
stay energetic in our endeavors to discover and learn. Max
Perutz once said of his optimism and persistence in the face of
seemingly intractable difficulties toward his goal: “As always,
I was driven on by unrealistic expectations.” 3 He harnessed
new knowledge, information, and technological capacities to
meet those expectations. If there seem to be any advances in
global health or in prosperity that seem likewise unrealistic,
I would counter that momentum of the gains is with us, and
new discoveries and their applications continue to give us tre-
Our endeavors toward these discoveries and applications
will forever remain worthy of our most ambitious dreams.
Received January 19, 2010. Accepted for publication February 22,
Disclosure: Presented as the Presidential Address at the 58th Annual
Meeting of the American Society of Tropical Medicine and Hygiene,
Washington, DC, November 21, 2009.
1. Wellems TE , Josephs R , 1979 . Crystallization of deoxyhemoglobin
S by fiber alignment and fusion . J Mol Biol 135: 651 – 674 .
2. Wellems TE , Vassar RJ , Josephs R , 1981 . Polymorphic assemblies
of double strands of sickle cell hemoglobin. Manifold pathways of
deoxyhemoglobin S crystallization . J Mol Biol 153: 1011 – 1026 .
3. Judson HT , 1995 . The Eighth Day of Creation: Makers of a
Revolution in Biology . New York : Penguin Books .
4. Crowther JG , 1974 . The Cavendish Laboratory 1874–1974 . New
York : Science History Publications .
5. Thomas JM , 2004 . Max Perutz . Proc Am Philos Soc 148: 235 – 241 .
6. Ferry G , 2007 . Max Perutz and the Secret of Life . Cold Spring
Harbor, NY : Cold Spring Harbor Laboratory Press .
7. Perutz MF , 1949 . Recent developments in the x-ray study of hae-
moglobin . Roughton FJW , Kendrew JC , eds. Haemoglobin: A
Symposium Based on a Conference Held at Cambridge in June
1948 in Memory of Sir Joseph Barcroft . London : Butterworths
Scientific Publications , 135 – 147 .
8. Perutz MF , 1992 . Protein Structure: New Approaches to Diseases
and Therapy . New York : W.H. Freeman and Company .
9. Perutz MF , 1970 . Stereochemistry of cooperative effects in haemo-
globin . Nature 228: 726 – 734 .
10. Perutz MF , Lehmann H , 1968 . Molecular pathology of human hae-
moglobin . Nature 219: 902 – 909 .
11. Research Collaboratory for Structural Bioinformatics , 2008 .
Annual Report . Available at: http://www.pdb.org . Accessed
September 17, 2009.
12. Nollert P , Feese MD , Staker BL , Kim H , 2005 . Protein x-ray crys-
tallography in drug discovery . Gad SC , ed. Drug Discovery
Handbook (Pharmaceutical Development Series) . Hoboken,
NJ : Wiley-Interscience .
13. Ingram VM , 2002 . The birth of molecular biology: how biophysi-
cists and biochemists in the 1950s shaped a new science . Nature
419: 669 – 670 .
14. Perutz MF , 1996 . By what right do we invoke human rights ? Proc
Am Philos Soc 140: 135 – 147 .
15. Stokes DE , 1997 . Pasteur’s Quadrant: Basic Science and
Technological Innovation . Washington, DC : The Brookings
16. Morel CM , 2008 . Research, development and innovation on
neglected diseases: a developing country perspective . 57th
Annual Meeting of the American Society of Tropical Medicine
and Hygiene . Commemorative Fund Lecture , December 9,
2008, New Orleans, LA .
17. Bush V , 1945 . Science—the Endless Frontier . Available at: http://
www.nsf.gov/od/lpa/nsf50/vbush1945.htm . Accessed November
18. Pasteur L , 1872 . Pourquoi le goût de la vendange diffère de celui
du raisin . Vallery-Radot LP , ed. Oeuvres de Pasteur. Tome III.
Études sur le Vinaigre et sur le Vin (1924) . Paris : Masson (pub-
licly available at: http://gallica.bnf.fr/ ), 461 – 464 .
19. Pasteur L , 1871 . Pourquoi la France n’a pas trouvé d’hommes
supérieurs au moment du péril . Vallery-Radot LP , ed. Oeuvres
de Pasteur. Tome VII. Mélanges Scientifiques et Littéraires
(1939) . Paris : Masson (publicly available at: http://gallica.bnf
.fr/ ), 211 – 221 .
20. Pais A , 1991 . Niels Bohr’s Times, in Physics, Philosophy, and Polity .
Oxford : Clarendon Press .
21. de Hevesy G , 1944 . Some applications of isotopic indicators: Nobel
lecture, December 12, 1944 . Available at: http://nobelprize.org/
Accessed November 12, 2009.
22. Enea V , Ellis J , Zavala F , Arnot DE , Asavanich A , Masuda A ,
Quakyi I , Nussenzweig RS , 1984 . DNA cloning of Plasmodium
falciparum circumsporozoite gene: amino acid sequence of
repetitive epitope . Science 225: 628 – 630 .
23. Dame JB , Williams JL , McCutchan TF , Weber JL , Wirtz RA ,
Hockmeyer WT , Maloy WL , Haynes JD , Schneider I , Roberts
D , et al. , 1984 . Structure of the gene encoding the immunodomi-
nant surface antigen on the sporozoite of the human malaria
parasite Plasmodium falciparum . Science 225: 593 – 599 .
24. Wellems TE , Howard RJ , 1986 . Homologous genes encode two
distinct histidine-rich proteins in a cloned isolate of Plasmodium
falciparum . Proc Natl Acad Sci USA 83: 6065 – 6069 .
25. Maniatis T , Fritsch EF , Sambrook J , 1982 . Molecular Cloning: A
Laboratory Manual . Cold Spring Harbor, NY : Cold Spring
Harbor Laboratory Press .
26. Bohr N , 1932 . Light and life (Pt. 1) . Nature 133: 421 – 423 .
27. Bohr N , 1932 . Light and life (Pt. 2) . Nature 133: 457 – 459 .
6 Download full-text
28. Segrè G , 2007 . Faust in Copenhagen: A Struggle for the Soul of
Physics . New York : Penguin Group , 266 – 269 .
29. McKaughan DJ , 2005 . The influence of Niels Bohr on Max
Delbrück: revisiting the hopes inspired by “light and life” . Isis
96: 507 – 529 .
30. Delbrück M , 1969 . A physicist’s renewed look at biology–twenty
years later: Nobel lecture, December 10, 1969 . Available at:
delbruck-lecture.html . Accessed November 12, 2009.
31. Obama B , 2009 . Remarks by the President at the National
Academy of Sciences Annual Meeting, April 27, 2009 . Available
Meeting/ . Accessed November 12, 2009.
32. Committee on a New Biology for the 21st Century , 2009 . A New
Biology for the 21st Century: Ensuring the United States Leads
the Coming Biology Revolution . Washington, DC : The National
Academies Press . Available at: http://www.nap.edu/catalog/
12764.html . Accessed November 9, 2009.
33. Fermi G , Perutz MF , Shaanan B , Fourme R , 1984 . The crystal struc-
ture of human deoxyhaemoglobin at 1.74 A resolution . J Mol
Biol 175: 159 – 174 .