scholarly journals Primary Peptide Folding Dynamics Observed with Ultrafast Temperature Jump

2009 ◽  
Vol 121 (31) ◽  
pp. 5738-5742 ◽  
Author(s):  
Omar F. Mohammed ◽  
Gouri S. Jas ◽  
Milo M. Lin ◽  
Ahmed H. Zewail
Keyword(s):  
Temperature Jump ◽  
Peptide Folding ◽  
Folding Dynamics

scholarly journals Primary Peptide Folding Dynamics Observed with Ultrafast Temperature Jump

2009 ◽  
Vol 48 (31) ◽  
pp. 5628-5632 ◽  
Author(s):  
Omar F. Mohammed ◽  
Gouri S. Jas ◽  
Milo M. Lin ◽  
Ahmed H. Zewail
Keyword(s):  
Temperature Jump ◽  
Peptide Folding ◽  
Folding Dynamics

scholarly journals Impact ofβ-Turn Sequence onβ-Hairpin Dynamics Studied with Infrared-Detected Temperature Jump

2012 ◽  
Vol 27 ◽  
pp. 557-564 ◽  
Author(s):  
Alexander Popp ◽  
Ling Wu ◽  
Timothy A. Keiderling ◽  
Karin Hauser
Keyword(s):  
Thermodynamic Stability ◽  
Temperature Jump ◽  
Relaxation Dynamics ◽  
State Behavior ◽  
Time Constants ◽  
Disordered Structure ◽  
Folding Dynamics ◽  
Ir Detection ◽  
Tryptophan Zipper

Folding dynamics forβ-structure loss and disordered structure gain were studied in a modelβ-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG) turn sequence, that is, SWTWETGKWTWK, using laser-induced temperature-jump (T-jump) kinetics with IR detection. As has been shown previously, the TG turn sequence reduces the thermodynamicβ-hairpin stability as compared to the Asn-Gly sequence used in Trpzip2 (TZ2-NG). In this study, we found that the TG-turn slows down the overall relaxation dynamics as compared to TZ2-NG, which were studied at higher temperatures where the time constants show little difference between relaxation of theβ-strand and the disordered conformation. These time constants become equivalent at lower temperatures for TZ2-TG than was seen for TZ2-NG. The correlation of thermodynamic stability and rates of relaxation suggests that the change from NG to TG turn results in a slowing of folding, lowerkf, with less change of the unfolding rate,ku, assuming two state behavior at higher temperatures.

scholarly journals Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump

2004 ◽  
Vol 101 (11) ◽  
pp. 3809-3814 ◽  
Author(s):  
G. Dimitriadis ◽  
A. Drysdale ◽  
J. K. Myers ◽  
P. Arora ◽  
S. E. Radford ◽  
...  
Keyword(s):  
Temperature Jump ◽  
Protein A ◽  
Staphylococcal Protein A ◽  
Staphylococcal Protein ◽  
Folding Dynamics

Peptide Folding Dynamics:  A Time-Resolved Study from the Nanosecond to the Microsecond Time Regime

2006 ◽  
Vol 110 (45) ◽  
pp. 22834-22841 ◽  
Author(s):  
Mariano Venanzi ◽  
Emanuela Gatto ◽  
Gianfranco Bocchinfuso ◽  
Antonio Palleschi ◽  
Lorenzo Stella ◽  
...  
Keyword(s):  
Peptide Folding ◽  
Time Resolved ◽  
Time Regime ◽  
Folding Dynamics

Coarse Master Equations for Peptide Folding Dynamics†

2008 ◽  
Vol 112 (19) ◽  
pp. 6057-6069 ◽  
Author(s):  
Nicolae-Viorel Buchete ◽  
Gerhard Hummer
Keyword(s):  
Peptide Folding ◽  
Master Equations ◽  
Folding Dynamics

Residue Specific Resolution of Protein Folding Dynamics Using Isotope-Edited Infrared Temperature Jump Spectroscopy†

Biochemistry ◽  
2007 ◽  
Vol 46 (11) ◽  
pp. 3279-3285 ◽  
Author(s):  
Scott H. Brewer ◽  
Benben Song ◽  
Daniel P. Raleigh ◽  
R. Brian Dyer
Keyword(s):  
Protein Folding ◽  
Temperature Jump ◽  
Folding Dynamics

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

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