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Complete change of the protein folding transition state upon circular permutation
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Institutionen för datavetenskap.
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
2002 (Engelska)Ingår i: Nature Structural Biology, ISSN 1072-8368, Vol. 9, s. 818-22Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Reversing the loop lengths of the small protein S6 by circular permutation has a dramatic effect on the transition state structure: it changes from globally diffuse to locally condensed. The phenomenon arises from a biased dispersion of the contact energies. Stability data derived from point mutations throughout the S6 structure show that interactions between residues that are far apart in sequence are stronger than those that are close. This entropy compensation drives all parts of the protein to fold simultaneously and produces the diffuse transition-state structure typical for two-state proteins. In the circular permutant, where strong contacts and short sequence separations are engineered to concur, the transition state becomes atypically condensed and polarized. Taken together with earlier findings that S6 may also fold by a 'collapsed' trajectory with an intermediate, the results suggest that this protein may fold by a multiplicity of mechanisms. The observations indicate that the diffuse transition state of S6 is not required for folding but could be an evolutionary development to optimize cooperativity.

Ort, förlag, år, upplaga, sidor
2002. Vol. 9, s. 818-22
Identifikatorer
URN: urn:nbn:se:umu:diva-8790DOI: doi:10.1038/nsb847OAI: oai:DiVA.org:umu-8790DiVA, id: diva2:148461
Anmärkning
Jeanette HargboTillgänglig från: 2008-02-12 Skapad: 2008-02-12 Senast uppdaterad: 2018-06-09Bibliografiskt granskad
Ingår i avhandling
1. Protein Folding Studies on the Ribosomal Protein S6: the Role of Entropy in Nucleation
Öppna denna publikation i ny flik eller fönster >>Protein Folding Studies on the Ribosomal Protein S6: the Role of Entropy in Nucleation
2005 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

One of the most challenging tasks remaining in the field of biochemistry is the one of understanding how the information within the amino acid sequence of proteins translates into a unique structure. Solving this problem would lead to endless possibilities for application in the medical and biotechnology industry.

Many decades ago scientists realized that the process that facilitates the folding of a polypeptide chain could not be random and happen by chance; there needs to be direction in the folding free energy landscape. This landscape is defined by the thermodynamic factors entropy and enthalpy. The contribution made by enthalpy i.e. the contact energies from intra- and intermolecular interactions have been extensively investigated by various mutational studies. The influence of entropy on the other hand, is less well understood. My work focuses on the effect of altering the entropic components of forming the various parts of a known protein scaffold. This is done by genetic engineering in combination with biophysical characterisation and analysis. The results show effects on protein folding rates as well as on the pathway for nucleation and emphasis the ability of the folding landscape to readjust to entropic variations. Proteins are therefore not required to fold along a unique route to their final structure but can do so in several ways. The folding pathways we observe today have hence likely evolved as an adaptation to biological demands.

Ort, förlag, år, upplaga, sidor
Umeå: Kemi, 2005. s. 150
Nyckelord
Biochemistry, protein folding, circular permutation, topology, connectivity, entropy, protein stability, chevron plot, Biokemi
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
biokemi
Identifikatorer
urn:nbn:se:umu:diva-535 (URN)91-7305-890-4 (ISBN)
Disputation
2005-06-03, KB3A9, KBC, Umeå universitet, Umeå, 13:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2005-05-10 Skapad: 2005-05-10 Senast uppdaterad: 2009-08-13Bibliografiskt granskad

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