scholarly journals Do soft anions promote protein denaturation through binding interactions? A case study using ribonuclease A

RSC Advances ◽  
2019 ◽  
Vol 9 (6) ◽  
pp. 3416-3428 ◽  
Author(s):  
Olga A. Francisco ◽  
Courtney J. Clark ◽  
Hayden M. Glor ◽  
Mazdak Khajehpour
Keyword(s):  
Protein Folding ◽  
Protein Denaturation ◽  
Ribonuclease A ◽  
Binding Interactions

Soft anions promote protein folding through binding backbone CH and CH2 groups.

scholarly journals Protein folding stability and binding interactions through the lens of evolution: a dynamical perspective

2021 ◽  
Vol 66 ◽  
pp. 207-215
Author(s):  
Tushar Modi ◽  
Paul Campitelli ◽  
Ismail Can Kazan ◽  
Sefika Banu Ozkan
Keyword(s):  
Protein Folding ◽  
Binding Interactions

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

Process, Outcomes and Possible Elimination of Aggregation with Special Reference to Heme Proteins; Likely Remediations of Proteinopathies

2020 ◽  
Vol 21 (6) ◽  
pp. 573-583 ◽  
Author(s):  
Mohammad Furkan ◽  
Rizwan Hasan Khan
Keyword(s):  
Protein Folding ◽  
Protein Misfolding ◽  
Heme Proteins ◽  
Protein Denaturation ◽  
Natural Phenomenon ◽  
Three Dimension ◽  
Modern Biology ◽  
Major Life ◽  
Adverse Environmental Conditions

Protein folding is a natural phenomenon through which a linear polypeptide possessing necessary information attains three-dimension functionally active conformation. This is a complex and multistep process and therefore, the presence of several intermediary structures could be speculated as a result of protein folding. In in vivo, this folding process is governed by the assistance of other proteins called molecular chaperones and heat shock proteins. Due to the mechanism of protein folding, these intermediary structures remain major challenge for modern biology. Mutation in gene encoding amino acid can cause adverse environmental conditions which may result in misfolding of the linear polypeptide followed by the formation of aggregates and amyloidosis. Aggregation contributes to the pathophysiology of several maladies including diabetes mellitus, Huntington’s and Alzheimer’s disease. The propensity of native structure to form aggregated and fibrillar assemblies is a hallmark of amyloidosis. During aggregation of a protein, transition from α helix to β sheet is observed, and mainly β sheeted structure is visualised in a mature fibril. Heme proteins are very crucial for major life activities like transport of oxygen and carbon dioxide, synthesis of ATP, role in electron transport chain, and detoxification of free radicals formed during biochemical reactions. Any structural variation in the heme proteins may lead to a fatal response. Hence characterization of the folding intermediates becomes crucial. The characterization has been deciphered with the help of strong denaturants like acetonitrile and TFE. Moreover, possible role of elimination of these aggregates and prevention of protein denaturation is also discussed. Current review deals with the basic process and mechanism of the protein folding in general and the ultimate outcomes of the protein misfolding. Since Native conformation of heme proteins is essential for some vital activities as listed above, we have discussed possible prevention of denaturation and aggregation of heme proteins such as Hb, cyt c, catalase & peroxidase.

scholarly journals Correlation between Protein Stability Cores and Protein Folding Kinetics: A Case Study on Pseudomonas aeruginosa Apo-Azurin

Structure ◽  
2006 ◽  
Vol 14 (9) ◽  
pp. 1401-1410 ◽  
Author(s):  
Mingzhi Chen ◽  
Corey J. Wilson ◽  
Yinghao Wu ◽  
Pernilla Wittung-Stafshede ◽  
Jianpeng Ma
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Protein Folding ◽  
Protein Stability ◽  
Folding Kinetics

scholarly journals Small Protein Folding using Weighted Ensemble Simulation: A Case Study of Trp-Cage

2013 ◽  
Vol 104 (2) ◽  
pp. 398a
Author(s):  
Ernesto Suarez ◽  
Andrew Petersen ◽  
Steven Lettieri ◽  
Daniel M. Zuckerman
Keyword(s):  
Protein Folding ◽  
Small Protein ◽  
Ensemble Simulation
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