On an 19 October:
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1988 The
Nobel Physics Prize to Lederman, Schwartz, and Steinberger
^top^
for the neutrino beam method and the
demonstration of the doublet structure of the leptons through
the discovery of the muon neutrino
The Royal Swedish Academy of
Sciences has decided to award the 1988 Nobel Prize in Physics
jointly to Leon Lederman, Batavia, Illinois, USA, Melvin
Schwartz, Mountain view, California, USA and Jack Steinberger,
Geneva, Switzerland, for the neutrino beam method and the
demonstration of the doublet structure of the leptons through
the discovery of the muon neutrino.
The 1988 Nobel Prize in Physics
is awarded for the neutrino beam method and the discoveries
made using this. The experiment was planned when the three
researchers were associated with Columbia University in New
York, and carried out using the Alternating Gradient Synchrotron
(AGS) at Brookhaven National Accelerator Laboratory on Long
Island, USA.
Leon Lederman is currently
Director of the Fermi National Laboratory in Batavia, near
Chicago, Illinois, where the world's largest proton accelerator
is situated.
Melvin Schwartz, formerly
professor at Columbia and Stanford Universities, is now president
of his own firm specializing in computer communications,
in Mountain View, California, USA.
Jack Steinberger, who is an
American citizen works since long ago as a Senior Physicist
at CERN, Geneva, Switzerland, where he has led a number of
large experiments in elementary particle physics, including
experiments that employ neutrino beams.
Summary
The work now rewarded was
carried out in the 1960s. It led to discoveries that opened
entirely new opportunities for research into the innermost
structure and dynamics of matter. Two great obstacles to
further progress in research into weak forces - one of nature's
four basic forces - were removed by the prizewinning work.
One of the obstacles was that there was previously no method
for the experimental study of weak forces at high energies.
The other was theoretically more fundamental, and was overcome
by the three researchers' discovery that there are at least
two kinds of neutrino. One belongs with the electron, the
other with the muon. The muon is a relatively heavy, charged
elementary particle which was discovered in cosmic radiation
during the 1930s. The view, now accepted, of the paired grouping
of elementary particles has its roots in the prizewinner's
discovery. Background information Neutrinos are almost ghostlike
constituents of matter. They can pass unaffected through
any wall, in fact all matter is transparent to them. During
the conversion of atomic nuclei at the center of the sun,
enormous quantities of neutrinos (which belong to the electron
family) are produced. They pass through the whole sun virtually
unhindered and stream continually from its surface in all
directions. Every human being is penetrated by sun neutrinos
at a rate of several billion per square centimeter per second,
day and night, without leaving any noticeable trace. Neutrinos
are inoffensive. They have no electrical charge and they
travel at the speed of light, or nearly. Whether they are
weightless or have a finite but small mass is one of today's
unsolved problems. The contribution now awarded consisted
among other things of transforming the ghostly neutrino into
an active tool of research. As well as in cosmic radiation,
neutrinos, which belong to the moon family, can be produced
in a multi~step process in particle accelerators, and this
is what the prizewinners utilized. Suitable accelerators
exist in some few laboratories throughout the world. Since
all matter is transparent to neutrinos, it is difficult to
measure their action. Neutrinos are, however, not wholly
inactive. In very rare cases a neutrino can score a random
direct hit or, more correctly, a near-miss, on a quark, a
pointlike particle within a nucleon (proton or neutron) in
the nucleus of an atom or on a similarly infinitesimal electron
in the outer shell of an atom. The rarity of such direct
hits implies that a single neutrino of moderate energy would
be able to pass unhindered through a wall of lead of a thickness
measured in light-years. In neutrino experiments the rarity
of the reactions is compensated for by the intensity of the
neutrino beam. Even in the first experiment, the number of
neutrinos was counted in hundreds of billions. The probability
of a hit also increases with the energy of the neutrinos.
The method of the prizewinners makes it possible to achieve
very high energies, limited only by the performance of the
proton accelerator. Neutrino beams can reveal the hard inner
parts of a proton in a way not dissimilar to that in which
X-rays reveal a person's skeleton.
When the neutrino beam method
was invented by the Columbia team at the beginning of the
1960s the quark concept was still unknown, and the method
has only later become important in quark research. Also of
later date is the experimental discovery of an entirely new
way for a neutrino to interact with an electron or a quark
in which it retains its own identity after impact. The classical
way of reacting implied that the neutrino was converted into
an electrically charged lepton (electron or muon), and this
was the reaction utilized by the prizewinners. The prizewinners'
experiment The very first experiment using a beam of high-energy
neutrinos originated in one of the daily coffee breaks at
the Pupin laboratory, where faculty and research students
would relax together for half an hour. In this stimulating
atmosphere around Nobel Prizewinners T.D. Lee, C.N. Yang
(Nobel prize for physics 1957) and others at the end of the
1950s, the need to find a feasible method of studying the
effect of weak forces at high energies was discussed. Hitherto
it had only been possible to study processes of radioactive
decay, spontaneous processes at necessarily relatively low
energies. Beams of all common particles (electrons, protons
and neutrons) were discussed. While these are relatively
simple to produce, they were found to be unusable for this
purpose. The apparently hopeless situation suddenly changed
when Melvin Schwartz proposed that it ought to be possible
to produce and use a beam of neutrinos.
During the next two years
he, together with Leon Lederman and Jack Steinberger, worked
on the proposal in order to achieve a sufficiently intense
beam of neutrinos free from all other types of particle,
and to design a detector for measuring neutrino reactions.
The group at Columbia also included G. Danby, J.M. Gaillard
and K. Goulianos and N. Mistry. The neutrinos in the Columbia
experiment were produced in the decay in the flight of charged
pi-mesons. In a first step protons were accelerated to high
velocities and directed at a target of the metal beryllium.
As the next step high-velocity pi-mesons were produced in
a forward-directed beam. Mesons are radioactive, and they
decayed into a muon and a neutrino each when allowed to travel
a path of free flight, which was set at 21 meters. In this
step high-energy neutrinos were produced as a forward-directed
beam, still containing quantities of leftover pi-mesons and
myons which had been formed at the same time. To eliminate
these unwanted particles completely from the beam, a 13.5~meter~thick
wall of steel was needed. The material came from scrapped
warships. The measuring device (detector) was built behind
the wall, which of course was transparent to the neutrinos.
So that the detector should not be entirely transparent,
it was thought best to build it as a 10-ton spark chamber,
then a new and fairly untested type. The detector consisted
of a large number of aluminum plates with spark gaps between
them. A muon or an electron produced by a neutrino in one
of the aluminum plates photographed its own track as a series
of sparks, using a special self-exposing device. A burning
problem had arisen at the time of the experiment regarding
the measurements of muon radioactive decay.
The measurement results, to
which Jack Steinberger and Bruno Pontecorvo among others
contributed, disagreed with accepted theoretical calculations.
The problem was addressed by many researchers, among them
G. Feinberg and T.D. Lee, as well as methodologically by
Pontecorvo, and they indicated that one way out of the dilemma
would be the existence of two entirely different types of
neutrino. If the neutrinos in the Columbia experiment beam
were identical to the neutrinos common in beta decay, the
reactions in the detector should convert the neutrino to
a fast electron as often as to a fast muon. On the other
hand only muons would result if there were two different
kinds of neutrino. The prizewinners and their collaborators
arranged their detector so that the cause of the spark tracks
could be interpreted. The results showed that only muons
were produced by the neutrinos in the beam, no electrons.
Thus there exists a new type of neutrino that forms an intimate
pair with the muon. Consequently the electron forms its own
delimited family with its neutrino. The discovery thus had
immediate consequences. Knowledge of the role of the family
concept and the great importance of the method within elementary
particle physics has grown during the time that has elapsed
since the discovery was made. A question that is still current
is whether or not small departures from strict family membership
occur.
Leon
M. Lederman Fermi National Accelerator Laboratory Batavia,
IL, born 1922
Melvin
Schwartz Digital Pathways Inc. Mountain View, CA, born
1932
Jack
Steinberger CERN Geneva, Switzerland born 1921
Detailed
presentation of the research.
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1988
The Nobel Chemistry Prize to Deisenhofer, Huber, and Michel
. ^top^
The Royal Swedish
Academy of Sciences has decided to
award the 1988 Nobel Prize in chemistry jointly to West Germans
Dr. Johann Deisenhofer, Howard Hughes Medical Institute,
Dallas, Texas, Professor Robert Huber, Max-Planck-Institut
für Biochemie, Martinsried, DBR, and Dr. Hartmut Michel,
Max-Planck-Institut für Biophysik, Frankfurt/Main, DBR.
for the determination of the three-dimensional structure
of a photosynthetic reaction center.
Photosynthesis - the most important chemical
reaction on earth
Summary
Johann Deisenhofer, Robert Huber and Hartmut
Michel are the first to succeed in unraveling the full
details of how a membrane-bound protein is built up, revealing
the structure of the molecule atom by atom. The protein is
taken from a bacterium which, like green plants and algae,
uses light energy from the sun to build organic substances.
All our nourishment has its origin in this process, which
is called photosynthesis and which is a condition for all
life on earth.
The organic substances serve as nourishment for both plants
and animals. Using the oxygen in the air, they consume these
nutrients through what is termed cellular respiration. The
conversion of energy in photosynthesis and cellular respiration
takes place through transport of electrons via a series of
proteins, which are bound in special membranes. These membrane-bound
proteins are difficult to obtain in a crystalline form that
makes it possible to determine their structure, but in 1982
Hartmut Michel succeeded in doing this. Determination
of the structure was then carried out in collaboration with
Johann Deisenhofer and Robert Huber between
1982 and 1985.
Photosynthesis in bacteria is simpler than in algae and higher
plants, but the work now rewarded has led to increased understanding
of photosynthesis in these organisms as well. Broader insights
have also been achieved into the problem how electrons can,
at an enormously high speed (in a billionth - 10-12
- of a second), be transferred in biological systems.
Background
Photosynthesis is the most important chemical reaction in
the biosphere, as it is the prerequisite for all higher life
on earth. In this process light from the sun is converted
into chemical energy, which is used as nutrition not only
by the photosynthetic organisms themselves but also by animals
which eat such organisms (e.g. cows eating grass), by other
living beings (e.g. humans) eating these animals, and so
on through the nutritional chain.
The energy necessary for life processes is to a large extent
liberated in the combustion of carbohydrate and fats by the
oxygen of the air in cellular respiration. This can, however,
continue indefinitely only because the nutritional substances
consumed are remade in the photosynthesis of green plants.
Here the plants build up, with aid of solar energy, complicated
organic compounds from two simple inorganic molecules, carbon
dioxide and water, with the concomitant liberation of oxygen.
Photosynthesis and respiration thus have as a result that
the sun drives a continuous cyclic process in the biosphere:
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A simpler form of photosynthesis, which leads to the formation
of organic material without liberation of oxygen, is found
in certain bacteria.
Photosynthesis and respiration comprise electron transfer
between proteins, which often contain metal ions, e.g. iron,
in specific electron-transport chains. The principles for
electron transfer between simple metallic compounds have
been analyzed in detail by the Nobel Prize winner for chemistry
in 1983, Henry
Taube. An important goal in the chemical research of
today is to extend these contributions in order to explain
electron transfer between the more complicated biochemical
molecules.
The electron-transport proteins in photosynthesis as well
as in respiration are organized as complicated molecular
aggregates bound to membrane systems of two specific cell
organelles, chloroplasts and mitochondria. The energy liberated
during the electron transport is used to pump protons across
the membranes, so that a difference in pH and electrical
potential between the two sides is created. This electrochemical
potential is then used to drive the synthesis of adenosine
triphosphate (ATP), the universal energy storage molecule
in living cells, according to the chemiosmotic mechanism
formulated by the British biochemist Peter
Mitchell (Nobel Prize for chemistry 1978).
Membrane-bound proteins are difficult to obtain in solution
and to purify to a form allowing a determination of their
detailed structure in three dimensions. Before 1984 there
were only fuzzy structural pictures of two membrane proteins
available. These pictures had been obtained by an electron
microscope technique developed by Aaron
Klug, the Nobel Prize winner for chemistry in 1982. The
situation changed drastically, however, in 1982, when Hartmut
Michel in systematic experiments succeeded in preparing
highly ordered crystals of a photosynthetic reaction center.
from a purple bacterium, allowing the determination of the
structure in atomic detail. The structural work was performed
in the period 1982-85 in collaboration with Johann Deisenhofer
and Robert Huber.
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Schematic illustration of a reaction
center. in a membrane in a photosynthesizing bacterium.
The figure shows how the photosynthetically active
components bacteriochlorophyll (BK), bacteriopheophytin
(BF), quinone (Q) and iron (Fe) and the haemgroups
of the cytocrome are arranged in the four proteins
forming the reaction center. |
As already
mentioned, the photosynthetic apparatus in bacteria is simpler
than in algae and higher plants. The structural work has,
however, shown that there is a close relationship between
the bacterial reaction center. and the oxygen-evolving protein
complex in higher plants, so that the structure determined
can be used also to increase our understanding of photosynthesis
in general. The structural picture agrees well with the order
of the electron transfer steps established earlier by more
indirect methods. The detailed structure now forms the basis
for more precise attempts to explain theoretically the course
of the individual chemical steps.
The structural determination rewarded has considerable chemical
importance far beyond the field of photosynthesis. Many central
biological functions in addition to photosynthesis and cell
respiration are associated with membrane-bound proteins.
Examples are transport of chemical substances between cells,
hormone action and nerve impulses. The structure of the reaction
center. has clarified the principles governing the three
dimensional structure of proteins spanning biological membranes,
e.g. ion pumps and other transport proteins. Thanks to the
method of crystallization developed by Hartmut Michel the
prospects of obtaining detailed structural information also
for other membrane proteins have improved. Not least important
is the fact that the reaction center. structure is an indispensable
tool in the attempts of theoretical chemists to understand
how electron transfer in biological systems can occur with
very high velocities (even in one billionth [US, trillionth]
of a second) across large distances (more than ten intervening
atoms) on the molecular scale.
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