Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins
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Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins (585 views)

Palmieri M, Malgieri G, Russo L, Baglivo I, Esposito S, Netti F, Del Gatto A, De Paola I, Zaccaro L, Pedone PV, Isernia C, Milardi D, Fattorusso R

J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2013 Apr 2; 135(13): 5220-5228.

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Paper type: Journal Article,

Impact factor: 11.444, 5-year impact factor: 11.015

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875797582&partnerID=40&md5=265e8956facb9aafd785c05d92042914

Keywords: Biological Process, Homologous Proteins, Intermediate State, Protein Folding Reaction, Protein Misfolding, Structural Feature, Thermal Unfolding, Zinc Finger Domains, Metal Ions, Random Processes, Thermodynamics, Zinc Compounds, Zinc Finger Protein, Article, Circular Dichroism, Differential Scanning Calorimetry, Molecular Mechanics, Nonhuman, Nuclear Magnetic Resonance, Prokaryotic Cell, Protein Structure, Magnetic Resonance Spectroscopy, Models,

Affiliations:
*** IBB - CNR ***

Department of Environmental, Biological and Pharmaceutical Science and Technology, Second University of Naples, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging-CNR (Naples), Via Mezzocannone 16, 80134 Naples, Italy


References:
Not available.
Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins

In the funneled landscape, proteins fold to their native states through a stochastic process in which the free energy decreases spontaneously and unfolded, transition, native, and possible intermediate states correspond to local minima or saddle points. Atomic description of the folding pathway appears therefore to be essential for a deep comprehension of the folding mechanism. In metallo-proteins, characterization of the folding pathways becomes even more complex, and therefore, despite their fundamental role in critical biological processes, little is known about their folding and assembly. The study of the mechanisms through which a cofactor influences the protein folding/unfolding reaction has been the rationale of the present study aimed at contributing to the search for cofactors' general roles in protein folding reactions. In particular, we have investigated the folding pathway of two homologous proteins, Ros87, which contains a prokaryotic zinc finger domain, and Ml4(52-151), lacking the zinc ion. Using a combination of CD, DSC and NMR techniques, we determined the thermodynamics and the structural features, at an atomic level, of the thermal unfolding of Ros87 and compared them to the behavior of Ml4(52-151). Our results, also corroborated by NMR H-1/H-2 exchange measurements, show that the presence of the structural Zn(II) in Ros87 implies a switch from the Ml4(52-151), fully cooperative to a two-step unfolding process in which the intermediate converts to the native state through a downhill barrierless transition. This observation, which has never been reported for any metal ion so far, may have a significant role in the understanding of the protein misfolding associated with the presence of metal ions, as observed in neurodegenerative diseases.
Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins

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Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins

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Total impact factor: 39.32 (33.856 excluding Abstracts).
Total 5 year impact factor: 37.669 (32.134 excluding Abstracts).

Last modified by Marco Comerci on Sunday 12 July 2020, 13:14:54
585 views. Last view on Thursday 20 March 2025, 23:56:01