Temperature effects on the nucleation mechanism of protein folding and on the barrierless thermal denaturation of a native protein

2008 ◽  
Vol 10 (41) ◽  
pp. 6281 ◽  
Author(s):  
Y. S. Djikaev ◽  
Eli Ruckenstein
Keyword(s):  
Protein Folding ◽  
Temperature Effects ◽  
Thermal Denaturation ◽  
Nucleation Mechanism ◽  
Native Protein

scholarly journals An Essential Nonredundant Role for Mycobacterial DnaK in Native Protein Folding

PLoS Genetics ◽  
2014 ◽  
Vol 10 (7) ◽  
pp. e1004516 ◽  
Author(s):  
Allison Fay ◽  
Michael S. Glickman
Keyword(s):  
Protein Folding ◽  
Native Protein

Protein folding

1977 ◽  
Vol 10 (3) ◽  
pp. 239-352 ◽  
Author(s):  
George Némethy ◽  
Harold A. Scheraga
Keyword(s):  
Protein Folding ◽  
Present Article ◽  
Polypeptide Chain ◽  
Three Dimensional ◽  
Native Protein ◽  
Recent Advances

This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the native protein. Experimental and theoretical aspects of protein folding have been reviewed by anfinsen & Scheraga (1975). In the present article, we emphasize advances made since the writing of that review, together with a brief summary of the background of recent studies.

scholarly journals Increased thermal stability of proteins in the presence of amino acids

1994 ◽  
Vol 303 (1) ◽  
pp. 147-153 ◽  
Author(s):  
S Taneja ◽  
F Ahmad
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cytochrome C ◽  
Thermal Denaturation ◽  
Thermal Transition ◽  
Native Protein ◽  
Guanidinium Chloride ◽  
Isoleucine Leucine ◽  
Hydrophobic Amino Acids ◽  
Thermal Stability Of

This study is a systematic attempt to understand the roles of osmolytes in protecting proteins against denaturing stress. Thermal denaturation of cytochrome c has been studied in the presence of various concentrations of all L-amino acids that are more hydrophobic than glycine and have a solubility of 0.1 M or higher in water at 25 degrees C. The basic observations are as follows. (1) Arginine and histidine destabilize the native protein; both Tm (the midpoint of thermal transition) and delta GDH2O (25 degrees C) (the Gibbs energy of stabilization) decrease with increasing amino acid concentration. (2) Isoleucine, leucine and phenylalanine have no effect on Tm and deltaGDH2O (25 degrees C). (3) Valine and less hydrophobic amino acids stabilize the protein in terms of Tm but deltaGDH2O (25 degrees C) is unchanged. This observation was confirmed by the study of isothermal denaturation of cytochrome c by guanidinium chloride which suggested that delta GDH2O is independent of osmolyte concentration, but Cm (the midpoint of transition) is increased in their presence. (4) In the case of stabilizers, change in Tm/mol of amino acid decreases with increasing hydrophobicity of these osmolytes.

19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate

Biochemistry ◽  
2013 ◽  
Vol 52 (34) ◽  
pp. 5780-5789 ◽  
Author(s):  
Julianne L. Kitevski-LeBlanc ◽  
Joshua Hoang ◽  
William Thach ◽  
Sacha Thierry Larda ◽  
R. Scott Prosser
Keyword(s):  
Protein Folding ◽  
19F Nmr ◽  
Folding Intermediate ◽  
Native Protein ◽  
Nmr Studies

scholarly journals 1P115 Fast thermal denaturation of the hyperthermophilic protein, ST1625 product(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S175
Author(s):  
Shuichiro Goda ◽  
Chihiro Morimoto ◽  
Chika Sakai ◽  
Harumi Yoshida ◽  
Haruhiko Sakuraba ◽  
...  
Keyword(s):  
Protein Folding ◽  
Thermal Denaturation ◽  
Poster Session ◽  
Meeting Program ◽  
Hyperthermophilic Protein
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