Carl-Ivar Brändén (1934–2004)

Jane Smith
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Abstract

Science lost a valued citizen on 28 April 2004 when Carl-Ivar BraÈndeÂn succumbed to lung cancer following an 18-month battle. BraÈndeÂn was a prominent member of the structural biology community. Carl grew up in Lapland in northern Sweden, where his father was the teacher in a one-room schoolhouse. His active and free childhood instilled a life-long love of exploration and nature. At the same time he developed a strong desire to expand his horizons beyond the frozen north, and decided that a good education was his ticket to rest of the world. This led him, from age 13 onward, to schooling away from his family and eventually to Uppsala University. Carl's higher education in science was characterized by an ability to take opportunities where and when he found them and by an intellect that was restless unless challenged with an important problem. He began studying mathematics and physics at Uppsala University, but, bored by the undergraduate physics curriculum and inspired by Linus Pauling's texts, he switched to chemistry. An early and important mentor was Professor Ingvar Lindqvist, who invited Carl into his laboratory for PhD studies in chemical crystallography. During his studies with Lindqvist, Carl co-authored a least-squares re®nement program for the ®rst Swedish electronic computer and used it to re®ne the structures of several metal coordination complexes he had solved. Again bored and on the verge of leaving both crystallography and chemistry, Carl was enticed to the new ®eld of protein crystallography by a lecture course in biochemistry. Thus, he leapt at a postdoctoral opportunity to develop re®nement methods for myoglobin with John Kendrew at the MRC laboratory in Cambridge, UK, where in 1962 joined the ®rst generation of protein crystallographers. In the company of Max Perutz, John Kendrew, Francis Crick, Fred Sanger, Michael Rossmann, David Blow, Sydney Brenner, Aaron Klug, Lubert Stryer, Richard Henderson and many others, Carl experienced the heady early days of molecular and structural biology and celebrated the Nobel prizes to Crick, Watson and Wilkins, and to Perutz and Kendrew.
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2004年4月28日,科学失去了一位有价值的公民,卡尔·伊瓦尔BraÈndeÂn在与肺癌抗争了18个月后去世。BraÈndeÂn是结构生物学界的杰出成员。卡尔在瑞典北部的拉普兰长大,他的父亲是一所只有一间教室的学校里的老师。他活泼自由的童年让他终生热爱探索和大自然。与此同时,他萌生了一种强烈的愿望,想把自己的视野扩展到寒冷的北方以外,并认定良好的教育是他通往世界其他地方的入场券。这使得他从13岁开始离开家人去上学,最终进入了乌普萨拉大学。卡尔接受的高等科学教育的特点是,无论何时何地,只要发现机会,他就能抓住机会,而且除非遇到重大问题,否则他的智力是不安分的。他开始在乌普萨拉大学学习数学和物理,但由于厌倦了本科物理课程,又受到莱纳斯·鲍林课本的启发,他转向了化学。他早期的一位重要导师是Ingvar Lindqvist教授,他邀请卡尔到他的实验室攻读化学晶体学博士学位。在他的研究与Lindqvist,卡尔共同撰写了最小二乘重构程序的第一个瑞典电子计算机,并使用它来重构几个金属配合物的结构,他已经解决。再次感到无聊,在离开晶体学和化学的边缘,卡尔被生物化学的讲座课程吸引到蛋白质晶体学的新领域。因此,他抓住了一个博士后机会,与英国剑桥MRC实验室的John Kendrew一起开发肌红蛋白的re - nement方法,并于1962年加入了第一代蛋白质晶体学家。在Max Perutz、John Kendrew、Francis Crick、Fred Sanger、Michael Rossmann、David Blow、Sydney Brenner、Aaron Klug、Lubert Stryer、Richard Henderson和其他许多人的陪伴下,Carl经历了分子和结构生物学令人兴奋的早期,并庆祝了诺贝尔奖授予Crick、Watson和Wilkins,以及Perutz和Kendrew。
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来源期刊
自引率
13.60%
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0
审稿时长
3 months
期刊介绍: Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.
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