Inaugural Lecture of Professor El-Kabbani El

Inaugural Lecture of Professor El-Kabbani
El-Kabbani 教授着任記念講演 Part 1 of 2
Tokuron Seminar 基盤医学特論
OMICS Course 特徴あるプログラム「オミクス解析学」
Structural Genomics:
Determination of the Three-Dimensional Structures of Proteins
構造遺伝学：タンパク質の 3 次構造決定
Prof Ossama El-Kabbani,
PhD
Office of International Affairs
Nagoya University Graduate
School of Medicine
Dr El-Kabbani received a PhD degree in structural biology from the
University of Saskatchewan (Canada) in 1987 followed by a
Postdoctoral appointment at Argonne National Laboratory (USA).
In 1989 he took up an Assistant Professor position at the Unversity
of Alabama in Birmingham. He moved to Monash University
(Australia) in 1996 to establish the Macromolecular X-Ray
Diffraction Facility at the College of Pharmacy. His contribution to
the structural biology field included the 3D structure determinations
of enzyme complexes at high resolution using synchrotron
radiation. He is currently a Professor at Nagoya University
Graduate School of Medicine.
Abstract — This seminar will describe the experimental and
analytical techniques that are used to determine the structures of
proteins. The topics covered will include the physical factors
contributing to the three-dimensional structures of proteins,
experimental and computer-aided methods for determining protein
structures, and high-throughput methods for elucidating the
structures of thousands of proteins. The ultimate goal of structural
genomics is to determine the three-dimensional structures of all
known gene products. Most structural-genomics programs further
restrict their goals by concentrating on water-soluble proteins,
whose structures are easier to determine with the current
technologies. The structural-genomics community anticipates that
once the structures of a critical number of “template” proteins are
known, it will become more possible to elucidate the structures of
other proteins on the basis of the similarity of their sequences to
those of the templates. The structure of a protein reflects the
protein’s function. Understanding the structure–function
relationship of a protein yields insights that can be of great practical
value. For instance, understanding the shape of a binding site on
an enzyme implicated in a disease can help a drug company design
a molecule that acts as a specific inhibitor of this enzyme. To
understand how proteins achieve the tremendous diversity of
structures that gives rise to so many different functions, it is
important that we learn about their chemical properties.
Time & Place
日時・場所
4 June 2015 (Thu) 17:00-18:30
Meeting Room 1,
1st Fl., Basic Medical Research Bldg.
2015 年 6 月 4 日 (木) 17:00-18:30
基礎研究棟
1 階会議室
[Notice] No registration required.
[Language] English
[注意] 事前申し込みは不要です。
[言語] 英語
関係講座・部門等の連絡担当者国際連携室下畑(内線 5408)
O f f i c e o f I n t e r n a t i o n a l A f f a i r s , S h i m o h a t a ( Ex t 5 4 0 8 )

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