Related Research Articles
Structural biology is a field that is many centuries old which, as defined by the Journal of Structural Biology, deals with structural analysis of living material at every level of organization. Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity and through magnifying glasses and light microscopes.
Biophysics is an interdisciplinary science that applies approaches and methods traditionally used in physics to study biological phenomena. Biophysics covers all scales of biological organization, from molecular to organismic and populations. Biophysical research shares significant overlap with biochemistry, molecular biology, physical chemistry, physiology, nanotechnology, bioengineering, computational biology, biomechanics, developmental biology and systems biology.
Johann Deisenhofer is a German biochemist who, along with Hartmut Michel and Robert Huber, received the Nobel Prize for Chemistry in 1988 for their determination of the first crystal structure of an integral membrane protein, a membrane-bound complex of proteins and co-factors that is essential to photosynthesis.
Hartmut Michel is a German biochemist, who received the 1988 Nobel Prize in Chemistry for determination of the first crystal structure of an integral membrane protein, a membrane-bound complex of proteins and co-factors that is essential to photosynthesis.
Frederic Middlebrook Richards, commonly referred to as Fred Richards, was an American biochemist and biophysicist known for solving the pioneering crystal structure of the ribonuclease S enzyme in 1967 and for defining the concept of solvent-accessible surface. He contributed many key experimental and theoretical results and developed new methods, garnering over 20,000 journal citations in several quite distinct research areas. In addition to the protein crystallography and biochemistry of ribonuclease S, these included solvent accessibility and internal packing of proteins, the first side-chain rotamer library, high-pressure crystallography, new types of chemical tags such as biotin/avidin, the nuclear magnetic resonance (NMR) chemical shift index, and structural and biophysical characterization of the effects of mutations.
Richard Henderson is a British molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.„Thanks to his work, we can look at individual atoms of living nature, thanks to cryo-electron microscopes we can see details without destroying samples, and for this he won the Nobel Prize in Chemistry."
Eva Nogales is a Spanish-American biophysicist at the Lawrence Berkeley National Laboratory and a professor at the University of California, Berkeley, where she served as head of the Division of Biochemistry, Biophysics and Structural Biology of the Department of Molecular and Cell Biology (2015–2020). She is a Howard Hughes Medical Institute investigator.
Gregory A. Petsko is an American biochemist and member of the National Academy of Sciences, the National Academy of Medicine, the American Academy of Arts and Sciences, and the American Philosophical Society. He is currently Professor of Neurology at the Ann Romney Center for Neurologic Diseases at Harvard Medical School and Brigham and Women's Hospital. He formerly had an endowed professorship in Neurology and Neuroscience at Weill Cornell Medical College and is still an adjunct professor of Biomedical Engineering at Cornell University, and is also the Gyula and Katica Tauber Professor, Emeritus, in biochemistry and chemistry at Brandeis University.
Professor Nils Gunnar Hansson von Heijne, born 10 June 1951 in Gothenburg, is a Swedish scientist working on signal peptides, membrane proteins and bioinformatics at the Stockholm Center for Biomembrane Research at Stockholm University.
Time resolved crystallography utilizes X-ray crystallography imaging to visualize reactions in four dimensions. This enables the studies of dynamical changes that occur in for example enzymes during their catalysis. The time dimension is incorporated by triggering the reaction of interest in the crystal prior to X-ray exposure, and then collecting the diffraction patterns at different time delays. In order to study these dynamical properties of macromolecules three criteria must be met;
S. Samar Hasnain FInstP, FRSC, is the inaugural Max Perutz professor of Molecular Biophysics at the University of Liverpool. In 1991 he became a Fellow of the Institute of Physics and in 2002 he became a Fellow of the Royal Society of Chemistry. In 1997 he became a Fellow of the Third World Academy of Sciences. He became Foreign Fellows of Pakistan Academy of Sciences in 2017.
Gabriel Waksman FMedSci, FRS, is Courtauld professor of biochemistry and molecular biology at University College London (UCL), and professor of structural and molecular biology at Birkbeck College, University of London. He is the director of the Institute of Structural and Molecular Biology (ISMB) at UCL and Birkbeck, head of the Department of Structural and Molecular Biology at UCL, and head of the Department of Biological Sciences at Birkbeck.
John Charles Howorth Spence ForMemRS HonFRMS was Richard Snell Professor of Physics at Arizona State University and Director of Science at the National Science Foundation BioXFEL Science and Technology Center.
Sir David Ian Stuart is a Medical Research Council Professor of Structural Biology at the Wellcome Trust Centre for Human Genetics at the University of Oxford where he is also a Fellow of Hertford College, Oxford. He is best known for his contributions to the X-ray crystallography of viruses, in particular for determining the structures of foot-and-mouth disease virus, bluetongue virus and the membrane-containing phages PRD1 and PM2. He is also director of Instruct and Life Sciences Director at Diamond Light Source.
Kanakaraj Sekar is an Indian bioinformatician and a professor at the Department of Computational and Data Sciences of the Indian Institute of Science (IISc). Known for his studies in the field of bioinformatics, Sekar heads the Laboratory for Structural Biology and Bio-computing at IISc. The Department of Biotechnology of the Government of India awarded him the National Bioscience Award for Career Development, one of the highest Indian science awards, for his contributions to biosciences in 2004.
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization.
Serial femtosecond crystallography (SFX) is a form of X-ray crystallography developed for use at X-ray free-electron lasers (XFELs). Single pulses at free-electron lasers are bright enough to generate resolvable Bragg diffraction from sub-micron crystals. However, these pulses also destroy the crystals, meaning that a full data set involves collecting diffraction from many crystals. This method of data collection is referred to as serial, referencing a row of crystals streaming across the X-ray beam, one at a time.
Henry N. Chapman FRS is a British physicist and the founding director of the Center for Free-Electron Laser Science at the German Electron Synchrotron (DESY). He has made numerous contributions to the field of x-ray coherent diffraction imaging and is a pioneer of the diffraction before destruction technique that allows to analyze biological samples with intense, ultrafast x-ray light, such as Photosystem II, a key macromolecule in photosynthesis.
Timothy John Richmond is an American molecular biologist, biochemist, and biophysicist.
Janos Hajdu is a Hungarian biophysicist. He is a professor of molecular biophysics at Uppsala University and a senior scientist at the Extreme Light Infrastructure beamline.
References
- ↑ Marx, Vivien (2014-08-28). "Richard Neutze". Nature Methods. 11 (9): 877. doi: 10.1038/nmeth.3074 . ISSN 1548-7091. PMID 25317451. S2CID 42058880.
- ↑ Neutze, Richard; Wouts, Remco; van der Spoel, David; Weckert, Edgar; Hajdu, Janos (2000-08-17). "Potential for biomolecular imaging with femtosecond X-ray pulses". Nature. 406 (6797): 752–757. Bibcode:2000Natur.406..752N. doi:10.1038/35021099. ISSN 0028-0836. PMID 10963603. S2CID 4300920.
- ↑ Martin-Garcia, Jose M.; Conrad, Chelsie E.; Coe, Jesse; Roy-Chowdhury, Shatabdi; Fromme, Petra (2016-07-15). "Serial femtosecond crystallography: A revolution in structural biology". Archives of Biochemistry and Biophysics. 602: 32–47. doi:10.1016/j.abb.2016.03.036. PMC 4909539 . PMID 27143509.
- ↑ Neutze, Richard (1995). Acceleration and optical interferometry (PhD thesis). UC Research Repository, University of Canterbury. hdl:10092/6569.
- ↑ Biochemistry; Zeel, New; Science. "With a passion for biochemistry". Science Faculty Magazine. Retrieved 2022-04-21.
- ↑ "The Young Scientist Award goes to Claudia Dallera". www.esrf.fr. Retrieved 2022-04-21.
- ↑ "Theorell-priset". Svenska Kemisamfundet (in Swedish). Retrieved 2022-04-21.