title: Role of water in protein folding, oligomerization, amyloidosis and miniprotein.
abstract: The essential involvement of water in most fundamental extra-cellular and intracellular processes of proteins is critically reviewed and evaluated in this article. The role of water in protein behavior displays structural ambivalence; it can protect the disordered peptide-chain by hydration or helps the globular chain-folding, but promotes also the protein aggregation, as well (see: diseases). A variety of amyloid diseases begins as benign protein monomers but develops then into toxic amyloid aggregates of fibrils. Our incomplete knowledge of this process emphasizes the essential need to reveal the principles of governing this oligomerization. To understand the biophysical basis of the simpler in vitro amyloid formation may help to decipher also the in vivo way. Nevertheless, to ignore the central role of the water's effect among these events means to receive an uncompleted picture of the true phenomenon. Therefore this review represents a stopgap role, because the most published studies--with a few exceptions--have been neglected the crucial importance of water in the protein research. The following questions are discussed from the water's viewpoint: (i) interactions between water and proteins, (ii) protein hydration/dehydration, (iii) folding of proteins and miniproteins, (iv) peptide/protein oligomerization, and (v) amyloidosis.
authors.affiliation: MTA-ELTE Protein Modelling Research Group, Eötvös Loránd University and Laboratory of Structural Chemistry & Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/A, Budapest, 1117, Hungary.
authors.forename: Tamás
authors.initials: T
authors.lastname: Vajda
authors.forename: András
authors.initials: A
authors.lastname: Perczel
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D058227:Amyloidogenic Proteins / Q000737:chemistry* / Q000378:metabolism; D000686:Amyloidosis / Q000378:metabolism*; D000818:Animals; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D066263:Protein Aggregation, Pathological / Q000378:metabolism*; D017510:Protein Folding; D055550:Protein Stability; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry / Q000378:metabolism
chemical_list: D000682:Amyloid; D058227:Amyloidogenic Proteins; D064267:Intrinsically Disordered Proteins; D010455:Peptides; C508725:Trp-cage peptide; D014867:Water; D003300:Copper; D015032:Zinc
keywords: amyloid fibrils; folding; miniproteins; oligomers; protein hydration