TY - JOUR AB - Proton detection developed in the last 20 years as the method of choice to study biomolecules in the solid state. In perdeuterated proteins, proton dipolar interactions are strongly attenuated, which allows yielding of high-resolution proton spectra. Perdeuteration and backsubstitution of exchangeable protons is essential if samples are rotated with MAS rotation frequencies below 60 kHz. Protonated samples can be investigated directly without spin dilution using proton detection methods in case the MAS frequency exceeds 110 kHz. This review summarizes labeling strategies and the spectroscopic methods to perform experiments that yield assignments, quantitative information on structure, and dynamics using perdeuterated samples. Techniques for solvent suppression, H/D exchange, and deuterium spectroscopy are discussed. Finally, experimental and theoretical results that allow estimation of the sensitivity of proton detected experiments as a function of the MAS frequency and the external B0 field in a perdeuterated environment are compiled. AU - Reif, B. C1 - 63712 C2 - 51500 SP - 10019-10035 TI - Deuteration for high-resolution detection of protons in protein magic angle spinning (MAS) solid-state NMR. JO - Chem. Rev. VL - 122 IS - 10 PY - 2022 SN - 0009-2665 ER - TY - JOUR AB - Membrane proteins (MPs) play essential roles in numerous cellular processes. Because around 70% of the currently marketed drugs target MPs, a detailed understanding of their structure, binding properties, and functional dynamics in a physiologically relevant environment is crucial for a more detailed understanding of this important protein class. We here summarize the benefits of using lipid nanodiscs for NMR structural investigations and provide a detailed overview of the currently used lipid nanodisc systems as well as their applications in solution-state NMR. Despite the increasing use of other structural methods for the structure determination of MPs in lipid nanodiscs, solution NMR turns out to be a versatile tool to probe a wide range of MP features, ranging from the structure determination of small to medium-sized MPs to probing ligand and partner protein binding as well as functionally relevant dynamical signatures in a lipid nanodisc setting. We will expand on these topics by discussing recent NMR studies with lipid nanodiscs and work out a key workflow for optimizing the nanodisc incorporation of an MP for subsequent NMR investigations. With this, we hope to provide a comprehensive background to enable an informed assessment of the applicability of lipid nanodiscs for NMR studies of a particular MP of interest. AU - Günsel, U.* AU - Hagn, F. C1 - 63462 C2 - 51319 SP - 9395-9421 TI - Lipid nanodiscs for high-resolution NMR studies of membrane proteins. JO - Chem. Rev. VL - 122 IS - 10 PY - 2021 SN - 0009-2665 ER - TY - JOUR AU - Nozière, B.* AU - Kalberer, M.* AU - Claeys, M.* AU - Allan, J.* AU - D'Anna, B.* AU - Decesari, S.* AU - Finessi, E.* AU - Glasius, M.* AU - Grgić, I.* AU - Hamilton, J.F.* AU - Hoffmann, T.* AU - Iinuma, Y.* AU - Jaoui, M.* AU - Kahnt, A.* AU - Kampf, C.J.* AU - Kourtchev, I.* AU - Maenhaut, W.* AU - Marsden, N.* AU - Saarikoski, S.* AU - Schnelle-Kreis, J. AU - Surratt, J.D.* AU - Szidat, S.* AU - Szmigielski, R.* AU - Wisthaler, A.* C1 - 43274 C2 - 36282 CY - Washington SP - 3919-3983 TI - The molecular identification of organic compounds in the atmosphere: State of the art and challenges. JO - Chem. Rev. VL - 115 IS - 10 PB - Amer Chemical Soc PY - 2015 SN - 0009-2665 ER - TY - JOUR AB - The smallest viable unit of life is the cell. From bacteria to mammals, all cells use the same nucleic acid-based universal code for the maintenance and inheritance of genetic information. All life on earth probably started with a common ancestral cell approximately 4 billion years ago. Today, a huge diversity of organisms live on Earth, many of them still at the evolutionary stage of unicellular organisms, while others are life forms of high complexity with large cell numbers. The development of this diversity was driven by evolution, a process assuring survival and adaption of life to new environmental challenges. While the first evolutionary processes were probably very simple genetic changes, these processes gradually became more sophisticated with the development of higher eukaryotes. The remaining major part of the genome, including all coding genes, is transcribed by RNAPII. It was first assumed that RNAPII transcription might be limited to genomic loci that give rise to messenger RNA (mRNA) or other stable transcripts. AU - Eick, D. AU - Geyer, M.* C1 - 27794 C2 - 32816 SP - 8456-8490 TI - The RNA polymerase II Carboxy-Terminal Domain (CTD) code. JO - Chem. Rev. VL - 113 IS - 11 PB - Amer. Chemical Soc. PY - 2013 SN - 0009-2665 ER - TY - JOUR AU - Ntziachristos, V. AU - Razansky, D. C1 - 905 C2 - 27153 SP - 2783-2794 TI - Molecular imaging by means of multispectral optoacoustic tomography (MSOT). JO - Chem. Rev. VL - 110 IS - 5 PB - American Chemical Society PY - 2010 SN - 0009-2665 ER - TY - JOUR AB - Alternative splicing appears to be sciences' pessimist as nothing can reliably be identified along with its many other fundamental problems. On the brighter side, an optimism can still be seen as the splicing's noise provides material for selection of new and beneficial variants. The evolution of alternative splicing may allow various stages be fixed in different species. Specifically, the prevalence and function of alternative splicing is discussed. In addition, several other topics discussed include the evolution of exon-intron structure, the evolution of the alternative exon-intron structure and the functionality of nonconserved isoforms, the origin of alternative regions, the changes in alternative splicing after gene duplication, and lastly, the recognition of alternative exons and databases of alternative splicing. AU - Artamonova, I.I. AU - Gelfand, M.S.* C1 - 2649 C2 - 24905 SP - 3407-3430 TI - Comparative genomics and evolution of alternative splicing: The pessimists' science. JO - Chem. Rev. VL - 107 IS - 8 PB - American Chemical Society PY - 2007 SN - 0009-2665 ER - TY - JOUR AB - Genomic sequence must be associated with the course of genome annotation for it to become useful and comprehensible. Annotation are notes that contain information about the cellular role and mechanism of action of genes and their products. However, they are both faced with quantitative and qualitative challenges. Quantitative in the sense that it is quite impossible to annotate all proteins with our available resources, while facing qualitative problem as there will be no experimental evidence to annotate. Thus, the current status of modern procedures that are used for manual genome annotation are presented. In addition, computational methods and software infrastructure are also discussed which are used for analyzing protein function. Processes on the reduction of error level of automatically generated annotation are also described. Lastly, problems in gene prediction with the focus on improving the quality of functional inference are also detailed. AU - Frishman, D. C1 - 2650 C2 - 24907 SP - 3448-3466 TI - Protein annotation at genomic scale: the current status. JO - Chem. Rev. VL - 107 IS - 8 PB - American Chemical Society PY - 2007 SN - 0009-2665 ER - TY - JOUR AB - Martin Beyer received his diploma in physics in 1996 and a Ph.D. in physical chemistry in 1999 from TU Munich. With a Feodor Lynen fellowship from the Alexander von Humboldt foundation, he conducted postdoctoral research at UC Berkeley. In 2003, he received the Heinz Maier Leibnitz award jointly given by the Deutsche Forschungsgemeinschaft and the Bundesministerium für Bildung und Forschung. He finished his habilitation in 2004 and obtained the venia legendi in physical chemistry from TU Munich in the same year. Martin Beyer's research focuses on gas-phase ion chemistry of molecular and metal clusters, computational chemistry, and fundamental concepts in mechanochemistry. Hauke Clausen-Schaumann studied physics at the Technical University of Munich. In 1995, he joined the group of Prof. Hermann Gaub, for his diploma research about the adsorption of DNA to nano-structured cationic lipid membranes. In 1996, he moved to the Ludwig Maximilians University in Munich, where he started his Ph.D. research in the area of single-molecule force spectroscopy. During this time, he also served as scientific coordinator of the national competence center for nanoanalytics. In 2000, he obtained his Ph.D. from the Ludwig Maximilians University, for his work on DNA mechanics. After several years as a scientist and R&D manager for private companies and public research organizations, he joined the Munich University for Applied Sciences as a Professor for nanobiotechnology, in October 2004. His research interests concern the mechanical properties of biomolecules and chemical bonds, the development of force-based biochip technologies, as well as biomembranes and single-enzyme activity.   AU - Beyer, M.K.* AU - Clausen-Schaumann, H. C1 - 5053 C2 - 23055 SP - 2921-2932 TI - Mechanochemistry: The mechanical activation of covalent bonds. JO - Chem. Rev. VL - 105 IS - 8 PY - 2005 SN - 0009-2665 ER -