Protein folding is the physical process in which a polypeptide is synthesized by a ribosome from an unstable, random coil into a linear chain of amino acids, resulting in protein's three-dimensional structure. This is typically a 'folded' conformation, by which the protein becomes biologically functional.
Susan Lee Lindquist, ForMemRS was an American professor of biology at MIT specializing in molecular biology, particularly the protein folding problem within a family of molecules known as heat-shock proteins, and prions. Lindquist was a member and former director of the Whitehead Institute and was awarded the National Medal of Science in 2010.
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis.
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the organellar proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively, due to their endosymbiotic origin.
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones.
The Max Planck Institute of Biochemistry is a research institute of the Max Planck Society located in Martinsried, a suburb of Munich. The institute was founded in 1973 by the merger of three formerly independent institutes: the Max Planck Institute of Biochemistry, the Max Planck Institute of Protein and Leather Research, and the Max Planck Institute of Cell Chemistry.
The heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. In a normal cell, proteostasis must be maintained because proteins are the main functional units of the cell. Many proteins take on a defined configuration in a process known as protein folding in order to perform their biological functions. If these structures are altered, critical processes could be affected, leading to cell damage or death. The heat shock response can be employed under stress to induce the expression of heat shock proteins (HSP), many of which are molecular chaperones, that help prevent or reverse protein misfolding and provide an environment for proper folding.
Co-chaperones are proteins that assist chaperones in protein folding and other functions. Co-chaperones are the non-client binding molecules that assist in protein folding mediated by Hsp70 and Hsp90. They are particularly essential in stimulation of the ATPase activity of these chaperone proteins. There are a great number of different co-chaperones however based on their domain structure most of them fall into two groups: J-domain proteins and tetratricopeptide repeats (TPR).
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.
The Dr. Paul Janssen Award for Biomedical Research is given annually by Johnson & Johnson to honor the work of an active scientist in academia, industry or a scientific institute in the field of biomedical research. It was established in 2004 and perpetuates the memory of Paul Janssen, the founder of Janssen Pharmaceutica, a Johnson & Johnson subsidiary.
Dame Carol Vivien Robinson, is a British chemist and former president of the Royal Society of Chemistry (2018–2020). She was a Royal Society Research Professor and is the Dr Lee's Professor of Physical and Theoretical Chemistry, and a professorial fellow at Exeter College, University of Oxford. She is the first director of the Kavli Institution for Nanoscience Discovery, University of Oxford, and she was previously professor of mass spectrometry at the chemistry department of the University of Cambridge.
The Heinrich Wieland Prize is awarded annually by the Boehringer Ingelheim Foundation for outstanding research on biologically active molecules and systems in the areas of chemistry, biochemistry and physiology as well as their clinical importance.
The Wiley Prize in Biomedical Sciences is intended to recognize breakthrough research in pure or applied life science research that is distinguished by its excellence, originality and impact on our understanding of biological systems and processes. The award may recognize a specific contribution or series of contributions that demonstrate the nominee's significant leadership in the development of research concepts or their clinical application. Particular emphasis will be placed on research that champions novel approaches and challenges accepted thinking in the biomedical sciences.
Proteostasis is the dynamic regulation of a balanced, functional proteome. The proteostasis network includes competing and integrated biological pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell. Loss of proteostasis is central to understanding the cause of diseases associated with excessive protein misfolding and degradation leading to loss-of-function phenotypes, as well as aggregation-associated degenerative disorders. Therapeutic restoration of proteostasis may treat or resolve these pathologies.
The Massry Prize was established in 1996, and was administered by the Meira and Shaul G. Massry Foundation until 2019. The Prize, of $40,000 and the Massry Lectureship, is bestowed upon scientists who have made substantial recent contributions in the biomedical sciences. Shaul G. Massry, M.D., who established the Massry Foundation, is Professor Emeritus of Medicine and Physiology and Biophysics at the Keck School of Medicine, University of Southern California. He served as Chief of its Division of Nephrology from 1974 to 2000. In 2009 the KECK School of Medicine was asked to administer the Prize, and has done so since that time. Ten winners of the Massry Prize have gone on to be awarded a Nobel Prize.
The Otto Warburg Medal is awarded annually by the German Society for Biochemistry and Molecular Biology to honour scientists who have contributed important work in the field of biological chemistry. It is named after Otto Warburg, a renowned German physiologist and Nobel Prize laureate. It was first awarded on his 80th birthday on 8 October 1963.
The Ernst Schering Prize is awarded annually by the Ernst Schering Foundation for especially outstanding basic research in the fields of medicine, biology or chemistry anywhere in the world. Established in 1991 by the Ernst Schering Research Foundation, and named after the German apothecary and industrialist, Ernst Christian Friedrich Schering, who founded the Schering Corporation, the prize is now worth €50,000.
Chaperones, also called molecular chaperones, are proteins that assist other proteins in assuming their three-dimensional fold, which is necessary for protein function. However, the fold of a protein is sensitive to environmental conditions, such as temperature and pH, and thus chaperones are needed to keep proteins in their functional fold across various environmental conditions. Chaperones are an integral part of a cell's protein quality control network by assisting in protein folding and are ubiquitous across diverse biological taxa. Since protein folding, and therefore protein function, is susceptible to environmental conditions, chaperones could represent an important cellular aspect of biodiversity and environmental tolerance by organisms living in hazardous conditions. Chaperones also affect the evolution of proteins in general, as many proteins fundamentally require chaperones to fold or are naturally prone to misfolding, and therefore mitigates protein aggregation.
T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates. TRiC is an example of a biological machine that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis.
Judith Frydman is a biochemist and the Donald Kennedy Chair in the School of Humanities & Sciences and Professor of Genetics at Stanford University. Her research focuses on protein folding.
