Special Issue "Protein Folding 2011"
Deadline for manuscript submissions: closed (30 April 2011)
Prof. Dr. Charles Gerday
Laboratory of Biochemistry, University of Liège, Institute of Chemistry, B6a, B-4000, Liège, Belgium
Interests: protein chemistry; enzymology; microbiology; molecular adaptations to low temperature; extremophiles
The folding of proteins is recognized as one of the most complex processes in Biochemistry since its understanding also implies the characterization, from the unfolded state, of all conformational changes such as intermediate and transition states that separate the unfolded polypeptide from its fully folded and active form. The situation is also rendered more complicated because most of the proteins are made of several domains all having their own thermodynamic and kinetics parameters of folding. Counter pressures are also exerted by the possible existence of disulfide bridges which have to be appropriately paired through oxidative processes driven by the Dsb disulfide bonds generation machinery implicating oxido-reductases and isomerases as well as by the existence of the cis- and trans- possible configuration of the peptide bonds immediately preceding the prolyl residues. This cis-trans isomerization is dependent on an ubiquitous class of foldases known as peptidyl-prolyl cis-trans isomerases. The folding of nascent polypeptides is also assisted by special proteins, known as chaperones that also play crucial roles in protecting proteins against irreversible misfolding possibly induced by various cellular stresses such as heat shock or cold shock for example. Although the existence of intermediates are not always required for efficient folding they are obviously generally essential in helping to restrict the conformational zones and to direct the molecule towards its final low energy state. They have been identified and monitored by stopped-flow techniques making use of chemical denaturants or physical methods such as pressure perturbation recently found to be quite able to precise the folding landscape of a protein that provides the basis of the understanding of protein folding.
The aim of this special issue is to illustrate, through selected examples, the progresses which has been recently made, both on theoretical and technical grounds, in the understanding of the folding process of proteins nowadays of crucial importance due to the discovery of the relationship existing between protein misfolding and various human diseases derived from neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease.
Prof. Dr. Charles Gerday
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed Open Access monthly journal published by MDPI.
- protein folding
- energy landscape
Int. J. Mol. Sci. 2010, 11(10), 4014-4034; doi:10.3390/ijms11104014
Received: 7 September 2010; in revised form: 1 October 2010 / Accepted: 9 October 2010 / Published: 19 October 2010| Download PDF Full-text (805 KB) | Download XML Full-text
Int. J. Mol. Sci. 2011, 12(4), 2294-2314; doi:10.3390/ijms12042294
Received: 1 March 2011; in revised form: 16 March 2011 / Accepted: 29 March 2011 / Published: 4 April 2011| Download PDF Full-text (725 KB) | Download XML Full-text
Int. J. Mol. Sci. 2011, 12(5), 2797-2807; doi:10.3390/ijms12052797
Received: 4 March 2011; in revised form: 7 April 2011 / Accepted: 12 April 2011 / Published: 28 April 2011| Download PDF Full-text (482 KB) | Download XML Full-text
Article: Acid-Denatured Green Fluorescent Protein (GFP) as Model Substrate to Study the Chaperone Activity of Protein Disulfide Isomerase
Int. J. Mol. Sci. 2011, 12(7), 4625-4636; doi:10.3390/ijms12074625
Received: 3 May 2011; in revised form: 17 June 2011 / Accepted: 4 July 2011 / Published: 18 July 2011| Download PDF Full-text (420 KB) | Download XML Full-text
Int. J. Mol. Sci. 2011, 12(8), 4850-4860; doi:10.3390/ijms11084850
Received: 7 April 2011; in revised form: 7 June 2011 / Accepted: 25 July 2011 / Published: 29 July 2011| Download PDF Full-text (648 KB) | Download XML Full-text
Review: FK506-Binding Protein 22 from a Psychrophilic Bacterium, a Cold Shock-Inducible Peptidyl Prolyl Isomerase with the Ability to Assist in Protein Folding
Int. J. Mol. Sci. 2011, 12(8), 5261-5284; doi:10.3390/ijms12085261
Received: 12 May 2011; in revised form: 28 July 2011 / Accepted: 9 August 2011 / Published: 17 August 2011| Download PDF Full-text (834 KB) | Download XML Full-text
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Type of Paper: Article
Title: Thermodynamics of Protein Folding
Author: Philippa Wiggins
Affiliation: 2/73 Newhaven Terrace, Mairangi Bay, Auckland, New Zealand; E-Mail: firstname.lastname@example.org
Abstract: Folding of proteins is considered in the light of their status as components of a solution in water with coexisting microdomains of high density water (HDW) and low density water (LDW). In their extended configuration they displace the equilibrium between LDW and HDW, thus incurring a large thermodynamic cost (DGW). Most hydrophobic proteins occupy microdomains of HDW, with few molecules in microdomains of LDW. Molecules in HDW fold to reduce their interface with HDW, their decrease in entropy being more than balanced by the concomitant decrease in DGW. Molecules in LDW do not fold. Most hydrophilic molecules occupy LDW microdomains with few molecules in HDW. Molecules in LDW fold, molecules in HDW do not.
Last update: 31 March 2011