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Executive Editor – Johannes Buchner

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Prof. Dr. Johannes Buchner

Executive Editor
Prof. Dr. Johannes Buchner

Vita & Research interests

Johannes Buchner received his PhD from the University of Regensburg, Germany, working with Rainer Jaenicke and Rainer Rudolph on different aspects of protein folding. During his postdoctoral stay at the NIH in Bethesda, USA in the group of Ira Pastan, he worked on immuno-toxins. From 1992 to 1998 he was an independent group leader at the University of Regensburg. Since 1998 he is full professor at the Technische Universität München, Munich, Germany. He is a member of the German Academy of Science, the Bavarian Academy of Science and of EMBO. He was awarded the Hans Neurath Award of the Protein Society, the Schleiden Medal of the Leopoldina and the Albrecht Kossel Award of the German Society of Chemistry, among others. Since 2014 he acts as Executive Editor for Biological Chemistry.

My Research interests:

  • Molecular chaperones
  • Protein folding in vivo
  • Heat shock response
  • Antibody structure and evolution

My perspective on Biological Chemistry:

Biological Chemistry aka “Hoppe-Seyler’s Zeitschrift für physiologische Chemie” is the oldest biochemical journal of the world. In its history of 140 years, many important findings were published in the pages of this journal, witnessing the progress in understanding the molecular basis of life.

It is a privilege to contribute to this proud tradition and to the journal’s continued dedication to cover the entire field of “physiological chemistry”. The broad scope is a challenge and an opportunity, especially in the context of a growing number of journals in this field. My goal is to help in providing timely and fair reviews of submitted manuscripts, pointing out the important issues to consider in improving the stories. In this context, the professional manuscript processing by the publisher is an asset both editors and authors enjoy.



The following papers are selected from those that have been handled by me as the responsible editor. I find them particularly interesting as explained below.

Biophysical analysis of three novel profilin-1 variants associated with amyotrophic lateral sclerosis indicates a correlation between their aggregation propensity and the structural features of their globular state

Edoardo Del Poggetto / Ludovica Gori / Fabrizio Chiti
DOI 10.1515/hsz-2016-0154

“The unspecific aggregation of variants of profilin, a protein involved in the organization of the cytoskeleton, is linked to amyotrophic lateral sclerosis. In this paper, the authors demonstrate that changes in stability of the protein, often associated with aggregation, do not contribute to this effect. Rather, structural perturbations of the native state play a key role. This sheds new light on an important question in the context of protein folding diseases.”

Troponins, intrinsic disorder, and cardiomyopathy

Insung Na / Min J. Kong / Shelby Straight / Jose R. Pinto / Vladimir N. Uversky
DOI 10.1515/hsz-2015-0303

“The troponin complex is important for cardiac muscle contraction. In this article, the authors study intrinsically disordered regions in the troponin subunits and the correlation with disease-causing mutations. This article provides an interesting twist for a well-studied phenomenon.”

Two new isoforms of the human hepatoma-derived growth factor interact with components of the cytoskeleton

Jessica Nüße / Ursula Mirastschijski / Mario Waespy / Janina Oetjen / Nadine Brandes / Osmond Rebello / Federico Paroni / Sørge Kelm / Frank Dietz
DOI 10.1515/hsz-2015-0273

“Although alternative splicing has been studied for a number of years, its consequences on protein function are largely uncharted territory. This study provides an interesting example where different splice forms of a growth factor lead to structural differences which affect its biological function by modulating the interaction with partners.”