Добавил:
ivanov666
Опубликованный материал нарушает ваши авторские права? Сообщите нам.
Вуз:
Предмет:
Файл:Великие ученые и изобретатели = Great Scientists and Inventors. Учебное пособие
.pdf
2. Соотнесите слова и словосочетания на английском языке с их
a) chemical synthesis
1) количественный анализ
b) sequence
2) аминокислота
c) diet
3) лабораторный стол
d) bond
4) твёрдая фаза
e) amino acid
5) последовательность; ряд; очередность
f) bench
6) изучение, исследование
g) exploration
7) питание, еда, корм; диета
h) solid phase
8) плодовитый изобретатель
i) quantitation
9) связь
j) prolific inventor
10) химический синтез
эквивалентами на русском языке.
3. Прочитайте следующие интернациональные слова и переведи-
те их на русский язык:
Medicine, laboratory, experiment, astronomy, protein, pharmacology, pyrimidine, dinucleotide, factor, synthesis, idea, progress, nucleotide, saccharide,
motivation, author, enzyme, journal, hormone, structure.
4. Ответьте на вопросы, не читая текст.
1. What is the purpose of biochemistry?
2. When do you think history of biochemistry began?
3. What do you know about methodology for chemical synthesis?
4. What modern trends within biochemistry are you acquainted with?
5. Прочтите текст и выполните послетекстовые задания.
Text
R. B. Merrifield was an American biochemist who won the Nobel Prize in
Chemistry in 1984 for the invention of solid phase peptide synthesis. Prize motivation: “for his development of methodology for chemical synthesis on a solid
matrix”.
61
He was born in Fort Worth, Texas, on 15 July 1921, the only son of
George E. Merrifield and Lorene Lucas. In 1923 the family moved to California
where he attended nine grade schools and two high schools before graduating
from Montebello High School in 1939. It was there that he developed an interest both in chemistry and in astronomy.
After two years at Pasadena Junior College he transferred to the University
of California at Los Angeles (UCLA). After graduation in chemistry he worked
for a year at the Philip R. Park Research Foundation taking care of an animal
colony and assisting with growth experiments on synthetic amino acid diets.
One of these was the experiment by Geiger that first demonstrated that the essential amino acids must be present simultaneously for growth to occur.
He returned to graduate school at the UCLA chemistry department with
professor of biochemistry M.S. Dunn to develop microbiological methods for
the quantitation of the pyrimidines. The day after graduating on 19 June 1949,
he married Elizabeth Furlong and the next day left for New York City and the
Rockefeller Institute for Medical Research.
At the Institute, later Rockefeller University, he worked as an Assistant for
Dr. D.W. Woolley on a dinucleotide growth factor he discovered in graduate
school and on peptide growth factors that Woolley had discovered earlier. These studies led to the need for peptide synthesis and, eventually, to the idea for
solid phase peptide synthesis (SPPS) in 1959. In 1963, he was sole author of a
classic paper in the Journal of the American Chemical Society in which he reported a method he called solid phase peptide synthesis, which is the fifth most
cited paper in the journal's history.
In the mid-60s Dr. Merrifieldʼs laboratory first synthesized bradykinin, angiotensin, desamino-oxytocin and insulin. In 1969, he and his colleague Bernd
Gutte announced the first synthesis of the enzyme, ribonuclease A. This work
proved the chemical nature of enzymes.
Dr. Merrifieldʼs method greatly stimulated progress in biochemistry,
pharmacology and medicine, making possible the systematic exploration of the
structural bases of the activities of enzymes, hormones and antibodies. The development and applications of the technique continued to occupy his laboratory,
62
where he remained active at the bench until recently. In 1993, he published his
autobiography, “Life during a Golden Age of Peptide Chemistry.” He received
the Association of Biomolecular Resource Facilities Award for outstanding
contributions to Biomolecular Technologies in 1998.
SPPS was subsequently used to synthesize ribonuclease A (with Bernd
Gutte). This achievement was all the more significant in that it demonstrated
that the linear sequence of amino acids joined in peptide bonds determined directly the tertiary structure of a peptide or protein. Information coded in one
dimension can directly determine the three dimensional structure of a molecule.
SPPS has been expanded to include solid phase synthesis of nucleotides
and saccharides.
Throughout his prolific career teaching and researching, Robert B. Merrifield has been honored with numerous national and international awards. He
was a Nobel Guest Professor at Uppsala University in 1968 and was elected a
member of the U.S. National Academy of Sciences in 1972. He has received
several awards for his work on peptide chemistry including the Lasker Award
for Basic Medical Research (1969), the Gairdner Award (1970), the IntraScience Award (1970), the American Chemical Society Award for Creative
Work in Synthetic Organic Chemistry (1972), the Nichols Medal (1973), the
Instrument Specialties Company Award of the University of Nebraska (1977),
and the 2nd Alan E. Pierce Award of the American Peptide Symposium (1979).
He has received honorary degrees from the University of Colorado (1969),
Uppsala University (1970), Yale University (1971), Newark College of Engineering (1972), the Medical College of Ohio (1972), Colgate University (1977),
and Boston College (1984). In 1984 he was appointed the John D. Rockefeller
Jr. Professor of the Rockefeller University.
After raising their six children, James, Nancy, Betsy, Cathy, Laurie and
Sally, his wife Elizabeth (Libby), a biologist by training, joined the Merrifield
laboratory at Rockefeller University where she worked for over 23 years.
After a long illness R. Bruce Merrifield died on May 14, 2006 at the age of
84 in his home in Cresskill, New Jersey. He is survived by his wife, children
and 16 grandchildren.
63
6. Соотнесите слова с их дефинициями:
1. Insulin is …
a) … a protein whose presence in the blood promotes
aldosterone secretion and tends to raise blood pressure.
2. Peptide is …
b) … a compound released in the blood in some circumstances that causes contraction of smooth muscle
and dilation of blood vessels. It is a peptide comprising
nine amino-acid residues.
3. Hormone is …
c) … a substance produced by a living organism which
acts as a catalyst to bring about a specific biochemical
reaction.
4. Bradykinin is …
d) … a hormone produced in the pancreas by the islets
of Langerhans that regulates the amount of glucose in
the blood.
5. Enzyme is …
e) … a blood protein produced in response to and
counteracting a specific antigen.
6. Angiotensin is …
f) … a regulatory substance produced in an organism
and transported in tissue fluids such as blood or sap to
stimulate specific cells or tissues into action.
7. Antibody is …
g) … a compound consisting of two or more amino acids linked in a chain.
8. Peptide bond is
…
h) … a compound consisting of a nucleoside linked to
a phosphate group.
9. Protein is …
i) nitrogen organic compound which has large molecules consisting of one or more long chains of amino
acids and is an important part of all living organisms,
especially as structural elements of muscle, hair, etc.,
and as enzymes and antibodies.
10. Nucleotide is …
j) … a chemical amide linkage, -NH-CO-, formed by
the condensation of the amino group of one amino acid
with the carboxyl group of another
64
7. Найдите в тексте следующие слова (номер абзаца указан
в скобках), определите, к какой части речи они относятся, и переве-
дите их.
solid (1); animal (3); assisting (3); demonstrated (3); quantitation (4);
growth (5); eventually (5); sole (5); progress (7); exploration (7); subsequently (8);
profile (11).
8. Заполните пропуски в предложениях, используя следующие
слова:
biochemist, led to, synthesized, method, throughout.
1. R. B. Merrifield was an American … who won the Nobel Prize in
Chemistry in 1984 for the invention of solid phase peptide synthesis.
2. These studies … the need for peptide synthesis and, eventually, to the
idea for solid phase peptide synthesis (SPPS) in 1959.
3. In the mid-60s Dr. Merrifieldʼs laboratory first … bradykinin, angioten-
sin, desamino-oxytocin and insulin.
4. Dr. Merrifieldʼs … greatly stimulated progress in biochemistry, pharmacology and medicine, making possible the systematic exploration of the structural bases of the activities of enzymes, hormones and antibodies.
5. … his prolific career teaching and researching, Robert B. Merrifield has
been honored with numerous national and international awards.
9. Составьте предложения из следующих слов:
1. Fort Worth / on / born / He / Texas / in / was /15 July 1921
2. there / he / was / developed / chemistry / interest / It / an / that / in
3. in / worked / graduation / chemistry / he / After / year / a / for / Philip R. /
the / at / Park Research Foundation
4. sole / was / a / paper / author / classic / He / in / of / Journal / of / the /
American / Chemical / Society / the
5. that / linear / the / demonstrated / sequence / It / acids / of / joined / amino / peptide / in / bonds
6. Robert / honored / been / with / B. Merrifield / numerous / national / has /
international / awards / and
65
7. expanded / include / solid / to / SPPS / been / phase / of / has / synthesis /
UNIT III
JACQUES DUBOCHET
and / saccharides / nucleotides
10. Найдите в тексте случаи употребления Participle II и объясни-
те их.
11. Подготовьте презентацию на тему “Robert Bruce Merrifield and
his discoveries”.
1. Study the following text. Try to understand all details. Consult a
dictionary if necessary. Point out the main idea of the text. Render the information of the text to your partner.
Text
Born in 1942 in Aigle, in the canton of Vaud, Jacques Dubochet spent a
good part of his childhood in the canton of Valais, in a milieu where Protestantism was an important part of life. His father, an engineer, built dams. His mother, who had a literary bent, dedicated herself to the four children. She was convinced that their third child would one day win the Nobel Prize. At the age of
12, Jacques was making telescopes in school while his classmates carved peanut bowls out of pieces of wood... “Iʼve always needed to understand how
things work to make my way through life. Itʼs as essential as eating,” he explains.
Since the late 1960’s, Jacques interest has been in the electron microscopy
(EM) study of DNA, and the development of EM techniques. He was the first to
harness the use of water in EM, which under normal circumstances would
66
evaporate, by discovering the process of water vitrification, applying this to
specimens, and developing electron cryo-microscopy (cryo-EM). This technique would revolutionise structural biology. By enabling specimens to be kept
in their natural state, not altered by dyes or fixatives, researchers could see
structures at unprecedented resolution. More recently, he has been involved in
the development of cryoEM of vitreous sections (CEMOVIS), which when
combined with computerised electron tomography for 3-D reconstruction, has
made it possible to see the atomic structure of large protein complexes.
Jacques studied physics at Lausanne and was awarded a degree in physical
engineering in 1967. He then studied for a Certificate in Molecular Biology at
the University of Geneva and undertook his PhD in biophysics at the University
of Geneva and University of Basel. In 1978 he started his group at the European
Molecular Biology Laboratory (EMBL) in Heidelberg. He moved to the University of Lausanne (UNIL) in 1987 as Professor of Biophysics, and became
Emeritus Professor when he retired in 2007. Jacques has received numerous
awards for his work, including EMBL’s Lennart Philipson Award in 2014 and
the Nobel Prize in Chemistry in 2017, jointly with Joachim Frank and the
LMB’s Richard Henderson, for the development of electron cryo-microscopy.
The Nobel Prize in Chemistry 2017 is awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules.
This method has moved biochemistry into a new era.
A picture is a key to understanding. Scientific breakthroughs often build
upon the successful visualisation of objects invisible to the human eye. However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery. Cryo-electron microscopy changes all of this. Researchers can
now freeze biomolecules mid-movement and visualise processes they have
never previously seen, which is decisive for both the basic understanding of
life’s chemistry and for the development of pharmaceuticals.
Working as a group leader at EMBL in Heidelberg in the 1980s Dubochet,
together with colleagues, developed a method to freeze thin layers of solutions
of enzymes or viruses without forming ice crystals – a technique known as vitrification. The team then studied these layers in an electron microscope, a de-
67
velopment that simplified the process of visualising biomolecules in solution. It
was the birth of cryo-electron microscopy, one of the cornerstones of modern
structural biology
“Jacques developed a technique that has had a tremendous impact on our
ability to determine the structure of molecules and understand their function,”
explains Iain Mattaj, EMBL Director General. “As one of the inventors of cryo-
electron microscopy sample preparation, it is fitting that his huge contributions
to research and technology innovation have been recognised by the Nobel
committee.”
Electron microscopes were long believed to only be suitable for imaging
dead matter, because the powerful electron beam destroys biological material.
But in 1990, Richard Henderson succeeded in using an electron microscope to
generate a three-dimensional image of a protein at atomic resolution. This
breakthrough proved the technology’s potential.
Joachim Frank made the technology generally applicable. Between 1975
and 1986 he developed an image processing method in which the electron mi-
croscope’s fuzzy twodimensional images are analysed and merged to reveal a
sharp three-dimensional structure.
Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled
water so rapidly that it solidified in its liquid form around a biological sample,
allowing the biomolecules to retain their natural shape even in a vacuum.
Following these discoveries, the electron microscope’s every nut and bolt
have been optimised. The desired atomic resolution was reached in 2013, and
researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of
everything from proteins that cause antibiotic resistance, to the surface of the
Zika virus. Biochemistry is now facing an explosive development and is all set
for an exciting future.
Dubochet and his teams have also developed important methods that built
on his invention, including a technique that enables the cutting of vitreous sections of high-pressure frozen tissue that allows the insides of cells to be imaged.
Today, cryo-EM is a method that EMBL makes available to scientists around
68
the world. Thanks to a new Imaging Technology Centre, set to be constructed at
EMBL at its site in Heidelberg, Germany, for external users, even more scientists will soon have access to this and other cutting-edge imaging technologies.
2. Подготовьте презентацию на тему “Robert Bruce Merrifield and
his discoveries”.
3. Найдите дополнительную информацию о Йоахиме Франке
и Ричарде Хендерсоне, подготовьте устное высказывание о их научной деятельности.
69
PART IV
UNIT I
NORBERT WIENER
(1894–1964)
THE FAMOUS SCIENTISTS IN THE FIELD
OF INFORMATION TECHNOLOGIES
(Texts for home reading)
1. Study the following text. Try to understand all details.
Consult a dictionary if necessary.
2. Point out the main idea of the text.
3. Render the information of the text to your partner.
Text
Norbert Wiener (November 26, 1894 – March 18, 1964) was an American
mathematician. He was Professor of Mathematics at MIT.
Later Wiener became a researcher in stochastic and noise processes, in the
field of electronic engineering, electronic communication, and control systems.
Wiener is considered the founder of cybernetics, a formalization of the notion of feedback in engineering, computer science, systems control, philosophy,
biology, and the organization of society.
Wiener won the Bôcher Memorial Prize in 1933 and the National Medal of
Science in 1963, presented by President Johnson at a White House Ceremony in
January, 1964, shortly before Wienerʼs death.
Wiener won the 1965 U.S. National Book Award in Science, Philosophy
and Religion.
70
Соседние файлы в предмете [НЕСОРТИРОВАННОЕ]