Titelbild: Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage (Angew. Chem. 46/2011)

2011 ◽  
Vol 123 (46) ◽  
pp. 10923-10923
Author(s):  
Robert M. Culik ◽  
Arnaldo L. Serrano ◽  
Michelle R. Bunagan ◽  
Feng Gai
Keyword(s):  
Protein Folding ◽  
Kinetic Measurements ◽  
Folding Mechanism

Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage

2011 ◽  
Vol 123 (46) ◽  
pp. 11076-11079 ◽  
Author(s):  
Robert M. Culik ◽  
Arnaldo L. Serrano ◽  
Michelle R. Bunagan ◽  
Feng Gai
Keyword(s):  
Protein Folding ◽  
Kinetic Measurements ◽  
Folding Mechanism

From Levinthal’s Paradox to the Effects of Cell Environmental Perturbation on Protein Folding

2020 ◽  
Vol 26 (42) ◽  
pp. 7537-7554 ◽  
Author(s):  
Juan Zeng ◽  
Zunnan Huang
Keyword(s):  
Protein Folding ◽  
Posttranslational Modifications ◽  
Three Dimensional ◽  
Rational Drug Design ◽  
Basic Knowledge ◽  
Sequence Evolution ◽  
3D Structures ◽  
Folding Mechanism ◽  
Cellular Environment ◽  
Environment Temperature

Background: The rapidly increasing number of known protein sequences calls for more efficient methods to predict the Three-Dimensional (3D) structures of proteins, thus providing basic knowledge for rational drug design. Understanding the folding mechanism of proteins is valuable for predicting their 3D structures and for designing proteins with new functions and medicinal applications. Levinthal’s paradox is that although the astronomical number of conformations possible even for proteins as small as 100 residues cannot be fully sampled, proteins in nature normally fold into the native state within timescales ranging from microseconds to hours. These conflicting results reveal that there are factors in organisms that can assist in protein folding. Methods: In this paper, we selected a crowded cell-like environment and temperature, and the top three Posttranslational Modifications (PTMs) as examples to show that Levinthal’s paradox does not reflect the folding mechanism of proteins. We then revealed the effects of these factors on protein folding. Results: The results summarized in this review indicate that a crowded cell-like environment, temperature, and the top three PTMs reshape the Free Energy Landscapes (FELs) of proteins, thereby regulating the folding process. The balance between entropy and enthalpy is the key to understanding the effect of the crowded cell-like environment and PTMs on protein folding. In addition, the stability/flexibility of proteins is regulated by temperature. Conclusion: This paper concludes that the cellular environment could directly intervene in protein folding. The long-term interactions of the cellular environment and sequence evolution may enable proteins to fold efficiently. Therefore, to correctly understand the folding mechanism of proteins, the effect of the cellular environment on protein folding should be considered.

scholarly journals How Does Mg 2+ Modulate the RNA Folding Mechanism: A Case Study of the G:C W:W Trans Basepair

2017 ◽  
Vol 113 (2) ◽  
pp. 277-289 ◽  
Author(s):  
Antarip Halder ◽  
Rohit Roy ◽  
Dhananjay Bhattacharyya ◽  
Abhijit Mitra
Keyword(s):  
Rna Folding ◽  
Folding Mechanism

Role of incompetent strata and geometry of faults on the folding mechanism, a case study: the Karun oil field in the Dezful Embayment, Iran

2019 ◽  
Vol 5 (4) ◽  
pp. 1781-1800
Author(s):  
Gh. Reza Asgari ◽  
Farzin Ghaemi ◽  
Bahman Soleimany ◽  
Behnam Rahimi ◽  
Younes Shekarian
Keyword(s):  
Oil Field ◽  
Dezful Embayment ◽  
Folding Mechanism

scholarly journals Simulations of the role of water in the protein-folding mechanism

2004 ◽  
Vol 101 (17) ◽  
pp. 6456-6461 ◽  
Author(s):  
Y. M. Rhee ◽  
E. J. Sorin ◽  
G. Jayachandran ◽  
E. Lindahl ◽  
V. S. Pande
Keyword(s):  
Protein Folding ◽  
Folding Mechanism
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