Molecular Chaperones in Cellular Protein Folding: Mechanisms and Pathways
نویسندگان
چکیده
منابع مشابه
Molecular chaperones--cellular machines for protein folding.
Proteins are linear polymers synthesized by ribosomes from activated amino acids. The product of this biosynthetic process is a polypeptide chain, which has to adopt the unique three-dimensional structure required for its function in the cell. In 1972, Christian Anfinsen was awarded the Nobel Prize for Chemistry for showing that this folding process is autonomous in that it does not require any...
متن کاملSpecial series: Molecular chaperones in protein folding and disease.
P ioneering work by Anfinsen established that the folding of a polypeptide is dictated by its primary sequence. The study of folding remains an active area of research and a question of emerging importance is how the special challenges imposed by the cytoplasm (e.g., high protein load, molecular crowding, and dynamic oligomerization) impact this process. Given the opportunities for off-pathway ...
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Protein folding is the process that leads from the linear amino acid sequence of a polypeptide chain to a defined spatial structure characteristic for the native protein. In 1961 Anfinsen showed that all the information needed for reaching the active 3D structure is encoded in the protein's amino acid sequence. Protein folding is initiated by collapse of the polypeptide chain, which is driven b...
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The early decades of Cell witnessed key discoveries that coalesced into the field of chaperones, protein folding, and protein quality control.
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Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases. Protein folding is a highly heterogeneous process and rarely populated intermediate states may play an important role. Single-molecule techniques are ideally suited to resolve these heterogeneities. In this thesis, I ...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2013
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.27.1_supplement.27.1