Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding

2021 ◽  
Author(s):  
Bridget Milorey ◽  
Harald Schwalbe ◽  
Nichole O’Neill ◽  
Reinhard Schweitzer-Stenner
Keyword(s):  
Protein Folding ◽  
Aspartic Acid ◽  
Early Protein ◽  
Unfolded State

scholarly journals Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics

2006 ◽  
Vol 15 (3) ◽  
pp. 564-582 ◽  
Author(s):  
Paul A. Ellison ◽  
Silvia Cavagnero
Keyword(s):  
Protein Folding ◽  
Folding Kinetics ◽  
Unfolded State

scholarly journals Slow Unfolded-State Structuring in Acyl-CoA Binding Protein Folding Revealed by Simulation and Experiment

2012 ◽  
Vol 134 (30) ◽  
pp. 12565-12577 ◽  
Author(s):  
Vincent A. Voelz ◽  
Marcus Jäger ◽  
Shuhuai Yao ◽  
Yujie Chen ◽  
Li Zhu ◽  
...  
Keyword(s):  
Protein Folding ◽  
Binding Protein ◽  
Unfolded State ◽  
Simulation And Experiment

scholarly journals Characterization of the Unfolded State Under Native Conditions: A Missing Piece of the Protein Folding Puzzle

2009 ◽  
Vol 96 (3) ◽  
pp. 220a
Author(s):  
Daniel P. Raleigh ◽  
Bing Shan ◽  
Wenli Meng ◽  
Jae-Hyun Cho ◽  
Humeyra Taskent
Keyword(s):  
Protein Folding ◽  
Unfolded State

Structural and Dynamic Characterization of the Acid-Unfolded State of hUBF HMG Box 1 Provides Clues for the Early Events in Protein Folding†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (22) ◽  
pp. 8117-8125 ◽  
Author(s):  
Xuecheng Zhang ◽  
Yingqi Xu ◽  
Jiahai Zhang ◽  
Jihui Wu ◽  
Yunyu Shi
Keyword(s):  
Protein Folding ◽  
Dynamic Characterization ◽  
Hmg Box ◽  
Unfolded State

scholarly journals Loops linking secondary structure elements affect the stability of molten globule intermediate state of apomyoglobin

2019 ◽  
Author(s):  
M.A. Majorina ◽  
B.S. Melnik
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Rate Constant ◽  
Intermediate State ◽  
Molten Globule ◽  
Protein Secondary Structure ◽  
Free Energies ◽  
Real Effect ◽  
Unfolded State ◽  
The Stability

AbstractApomyoglobin is a protein widely used as a model for studying globular protein folding. This work aimed to test the hypothesis on influence of rigidity and length of loops linking protein secondary structure elements on the stability of molten globule intermediate state. For this purpose, we studied folding/unfolding of mutant apomyoglobin forms with substitutions of proline residues to glycine and with loops elongated by three and six glycine residues. For all the protein forms, denaturation/renaturation kinetic curves at different urea concentrations were obtained, folding/unfolding constants were calculated and dependencies of rate constant logarithms on urea concentrations were plotted. All the data gave an opportunity to calculate free energies of different apomyoglobin states. As a result, the mutations in apomyoglobin loops were demonstrated to have a real effect on intermediate state stability compared to unfolded state.

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