Determination of intramolecular distance distribution during protein folding on the millisecond timescale

2000 ◽  
Vol 299 (5) ◽  
pp. 1363-1371 ◽  
Author(s):  
Vladimir Ratner ◽  
Michael Sinev ◽  
Elisha Haas
Keyword(s):  
Protein Folding ◽  
Distance Distribution ◽  
Intramolecular Distance

Determination of Ultrafast Protein Folding Rates from Loop Formation Dynamics

2005 ◽  
Vol 347 (3) ◽  
pp. 657-664 ◽  
Author(s):  
Marco Buscaglia ◽  
Jan Kubelka ◽  
William A. Eaton ◽  
James Hofrichter
Keyword(s):  
Protein Folding ◽  
Loop Formation ◽  
Folding Rates ◽  
Formation Dynamics

Determination of protein folding kinetic types using sequence and predicted secondary structure and solvent accessibility

Amino Acids ◽  
2010 ◽  
Vol 42 (1) ◽  
pp. 271-283 ◽  
Author(s):  
Hua Zhang ◽  
Tuo Zhang ◽  
Jianzhao Gao ◽  
Jishou Ruan ◽  
Shiyi Shen ◽  
...  
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Solvent Accessibility

The Influence of Dipeptide Composition on Protein Folding Rates

2011 ◽  
Vol 378-379 ◽  
pp. 157-160
Author(s):  
Jian Xiu Guo ◽  
Ni Ni Rao
Keyword(s):  
Protein Folding ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Dipeptide Composition ◽  
Coupling Effects ◽  
Jackknife Test ◽  
Folding Rates ◽  
Important Challenge ◽  
The Relationship

Understanding the relationship between amino acid sequences and folding rates of proteins is an important challenge in computational and molecular biology. All existing algorithms for predicting protein folding rates have never taken into account the sequence coupling effects. In this work, a novel algorithm was developed for predicting the protein folding rates from amino acid sequences. The prediction was achieved on the basis of dipeptide composition, in which the sequence coupling effects are explicitly included through a series of conditional probability elements. Based on a non-redundant dataset of 99 proteins, the proposed method was found to provide an excellent agreement between the predicted and experimental folding rates of proteins when evaluated with the jackknife test. The correlation coefficient was 87.7% and the standard error was 2.04, which indicated the important contribution from sequence coupling effects to the determination of protein folding rates.

Determination of distance distribution from time domain fluorometry

1989 ◽  
Vol 93 (24) ◽  
pp. 8013-8016 ◽  
Author(s):  
Sharon Albaugh ◽  
Robert F. Steiner
Keyword(s):  
Time Domain ◽  
Distance Distribution

scholarly journals An OGLE view of the bulge and Sagittarius

2013 ◽  
Vol 9 (S298) ◽  
pp. 415-415 ◽  
Author(s):  
Shoko Jin ◽  
Eva K. Grebel ◽  
Raoul Haschke
Keyword(s):  
Spatial Distribution ◽  
Dwarf Galaxy ◽  
Fourier Component ◽  
Distance Distribution ◽  
Light Curves ◽  
Line Of Sight ◽  
Galactic Centre ◽  
Galactic Bulge ◽  
First Time

AbstractWe use observations of OGLE-III ab-type RRLyrae stars towards the Galactic centre (Soszyński et al. 2011, AcA 6,1) to study the metallicity and 3D spatial distribution of the old and metal-poor component of the Galactic bulge. Metallicities and distances to the RRLyrae stars are derived photometrically from Fourier-component analyses of their light curves, allowing the determination of distances accurate to ~7% from 0 to 40 kpc. The distance distribution of the RRLyrae stars peaks at 8.8 kpc, with the data indicating the presence of a bar-like structure inclined at ~30° to the line of sight. The dataset also exhibits a secondary concentration of stars beyond the Galactic centre at ~27 kpc. This is consistent with the distance to the Sagittarius (Sgr) dwarf galaxy, and can be attributed to the serendipitous alignment of the Sgr stream with the bulge. This dataset allows the Sgr stream to be traced in this part of the sky for the first time. The underlying metallicity distributions are determined to have mean ± intrinsic width of [Fe/H]bulge = −1.24±0.23 dex and [Fe/H]Sgr = −1.53±0.14 dex.

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