scholarly journals Role of residual structure in the unfolded state of a thermophilic protein

2003 ◽  
Vol 100 (20) ◽  
pp. 11345-11349 ◽  
Author(s):  
S. Robic ◽  
M. Guzman-Casado ◽  
J. M. Sanchez-Ruiz ◽  
S. Marqusee
Keyword(s):  
Thermophilic Protein ◽  
Residual Structure ◽  
Unfolded State

Electrophoresis and Electrofocusing of Phytochrome from Etiolated Avena sativa L.

1989 ◽  
Vol 44 (1-2) ◽  
pp. 12-18 ◽  
Author(s):  
Rudolf Schendel ◽  
Wolfhart Rüdiger
Keyword(s):  
Isoelectric Focusing ◽  
Avena Sativa ◽  
Posttranslational Modification ◽  
Negative Charge ◽  
Native State ◽  
Signal Region ◽  
Unfolded State ◽  
Native Gel ◽  
Peptide Region

Abstract Phytochrome from etiolated oat seedlings (Avena sativa L.) was investigated by “native” gel electrophoresis and by isoelectric focusing. At pH 8 . 8 the Pfr form migrated faster than the Pr form in electrophoresis. We assume a difference in the surface charge rather than a difference in shape for the phytochrome forms. This assumption was confirmed by isoelectric focusing which clearly showed relatively more negative charge in the Pfr form than in the Pr form. The role of the peptide region from residue 323 to 360 is discussed in this connection. It carries 9 negatively charged residues, it is exposed only in the Pfr form and it has already been described as a signal region for rapid protein degradation (PEST sequence, see Rogers et al., Science 234, 364-368, 1986). The experiments on electrofocusing revealed a microheterogeneity of phytochrome which was present in the native state as well as in the completely unfolded state. The most probable reason could be either posttranslational modification or genetic polymorphism of phytochrome in oat.

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 The Role of the Unfolded State in Hairpin Stability

2003 ◽  
Vol 85 (6) ◽  
pp. 3513-3520 ◽  
Author(s):  
Hongxing Lei ◽  
Paul E. Smith
Keyword(s):  
Unfolded State

scholarly journals Tertiary Residual Structure of Myoglobin in the Acid-Unfolded State

1999 ◽  
Vol 39 (supplement) ◽  
pp. S164
Author(s):  
Y. Seki ◽  
S. Kidokoro ◽  
K. Soda
Keyword(s):  
Residual Structure ◽  
Unfolded State

Extreme Temperature Tolerance of a Hyperthermophilic Protein Coupled to Residual Structure in the Unfolded State

2008 ◽  
Vol 379 (4) ◽  
pp. 845-858 ◽  
Author(s):  
Marcus Wallgren ◽  
Jörgen Ådén ◽  
Olena Pylypenko ◽  
Therese Mikaelsson ◽  
Lennart B.-Å. Johansson ◽  
...  
Keyword(s):  
Extreme Temperature ◽  
Temperature Tolerance ◽  
Residual Structure ◽  
Unfolded State ◽  
Hyperthermophilic Protein

scholarly journals Role of Protein Stabilizers on the Conformation of the Unfolded State of Cytochromecand Its Early Folding Kinetics

2010 ◽  
Vol 285 (33) ◽  
pp. 25314-25323 ◽  
Author(s):  
Shubhasis Haldar ◽  
Samaresh Mitra ◽  
Krishnananda Chattopadhyay
Keyword(s):  
Folding Kinetics ◽  
Unfolded State

scholarly journals Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure

2017 ◽  
Vol 114 (37) ◽  
pp. 9882-9887 ◽  
Author(s):  
Basile I. M. Wicky ◽  
Sarah L. Shammas ◽  
Jane Clarke
Keyword(s):  
Structural Changes ◽  
Intrinsically Disordered Proteins ◽  
Disordered Proteins ◽  
Marginal Stability ◽  
Residual Structure ◽  
Intrinsically Disordered ◽  
Folded Proteins ◽  
The Stability ◽  
Ion Profiles

Intrinsically disordered proteins (IDPs) are characterized by a lack of defined structure. Instead, they populate ensembles of rapidly interconverting conformations with marginal structural stabilities. Changes in solution conditions such as temperature and crowding agents consequently affect IDPs more than their folded counterparts. Here we reveal that the residual structure content of IDPs is modulated both by ionic strength and by the type of ions present in solution. We show that these ion-specific structural changes result in binding affinity shifts of up to sixfold, which happen through alteration of both association and dissociation rates. These effects follow the Hofmeister series, but unlike the well-established effects on the stability of folded proteins, they already occur at low, hypotonic concentrations of salt. We attribute this sensitivity to the marginal stability of IDPs, which could have physiological implications given the role of IDPs in signaling, the asymmetric ion profiles of different cellular compartments, and the role of ions in biology.

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