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Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.
Protein folding is the physical process by which a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids. At this stage, the polypeptide lacks any stable three-dimensional structure. As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure.
Folding@home is a volunteer computing project aimed to help scientists develop new therapeutics for a variety of diseases by the means of simulating protein dynamics. This includes the process of protein folding and the movements of proteins, and is reliant on simulations run on volunteers' personal computers. Folding@home is currently based at the University of Pennsylvania and led by Greg Bowman, a former student of Vijay Pande.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a residue indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, cryo electron microscopy (cryo-EM) and dual polarisation interferometry to determine the structure of proteins.
In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, typically in the absence of its macromolecular interaction partners, such as other proteins or RNA. IDPs range from fully unstructured to partially structured and include random coil, molten globule-like aggregates, or flexible linkers in large multi-domain proteins. They are sometimes considered as a separate class of proteins along with globular, fibrous and membrane proteins.
Joel L. Sussman is an Israeli crystallographer best known for his studies on acetylcholinesterase, a key protein involved in transmission of nerve signals. He is the Morton and Gladys Pickman Professor of Structural Biology at the Weizmann Institute of Science in Rehovot and its director of the Israel Structural Proteomics Center.
Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology. It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence. The dogma was championed by the Nobel Prize Laureate Christian B. Anfinsen from his research on the folding of ribonuclease A. The postulate amounts to saying that, at the environmental conditions at which folding occurs, the native structure is a unique, stable and kinetically accessible minimum of the free energy. In other words, there are three conditions for formation of a unique protein structure:
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Arthur L. Horwich is an American biologist and Sterling Professor of Genetics and Pediatrics at the Yale School of Medicine. Horwich has also been a Howard Hughes Medical Institute investigator since 1990. His research into protein folding uncovered the action of chaperonins, protein complexes that assist the folding of other proteins; Horwich first published this work in 1989.
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David Wallach is a full professor at the Department of Biological Chemistry at Weizmann Institute of Science, Israel, laureate of the 2014 Emet Prize for Life Sciences. , and laureate of the 2018 The Paul Ehrlich and Ludwig Darmstaedter Prize.
Rohit Pappu is an Indian-born computational and theoretical biophysicist. He is the Gene K. Beare Distinguished Professor of Engineering and the director of the Center for Science & Engineering of Living Systems (CSELS) at Washington University in St. Louis.
Helen Jane Dyson is a British-born biophysicist and a professor of integrative structural and computational biology at the Scripps Research Institute in La Jolla, California. She is also currently editor-in-chief of the Biophysical Journal. She was elected a member of the National Academy of Sciences in 2022.
The dark proteome is defined as proteins with no defined three-dimensional structure. It can not be detected or analyzed with the use of homologous modeling or analytical quantification for the molecular conformation is unknown. Dark proteins are mostly composed of unknown unknowns
Michele Vendruscolo is an Italian British physicist working in the UK, noted for his theoretical and experimental work on protein folding, misfolding and aggregation.
Julie Forman-Kay is a scientist at the Hospital for Sick Children (SickKids) and professor at University of Toronto. Her research focuses on the dynamics, interactions, structures, and functions of intrinsically disordered proteins.
Gilad Haran is an Israeli biophysicist and physical chemist, a full professor at the Faculty of Chemistry in the Weizmann Institute of Science, and its former dean. An expert in molecular machines. Laureate of Weizmann Prize (2017) and Nakanishi Prize (2023).
References
- ↑ "Anna Elizabeth Rhoades". Yale Phonebook. Yale University.[ permanent dead link ]
- ↑ Ari Gafni, University of Michigan
- ↑ Gilad Haran, Weizmann Institute
- ↑ Rhoades E, Gussakovsky E, Haran G (March 2003). "Watching proteins fold one molecule at a time". Proc. Natl. Acad. Sci. U.S.A. 100 (6): 3197–202. Bibcode:2003PNAS..100.3197R. doi: 10.1073/pnas.2628068100 . PMC 152269 . PMID 12612345.
- ↑ Rhoades E, Cohen M, Schuler B, Haran G (November 2004). "Two-state folding observed in individual protein molecules". J. Am. Chem. Soc. 126 (45): 14686–7. CiteSeerX 10.1.1.702.7305 . doi:10.1021/ja046209k. PMID 15535670.
- ↑ Rhoades Lab, University of Pennsylvania
- ↑ "Elizabeth Rhoades to Receive 2019 BPS Michael and Kate Barany Award" . Retrieved 2020-02-02.
