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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/3567

Title: Protein folding, metal ions and conformational states: the case of a di-cluster ferredoxin
Authors: Leal, Sónia S.
Advisor: Gomes, Cláudio M.
Issue Date: 2010
Abstract: Metal ions are present in over thirty percent of known proteins. Apart from a well established function in catalysis and electron transfer, metals and metal centres are also important structural elements which may as well play a key role in modulating protein folding and stability. In this respect, cofactors can act not only as local structural stabilizing elements in the native state, contributing to the maintenance of a given specific structural fold, but may also function as potential nucleation points during the protein folding process...
Description: Dissertation presented to obtain the PhD degree in Biochemistry at the Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa
URI: http://hdl.handle.net/10362/3567
Appears in Collections:ITQB: PBFS - PhD Theses

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