World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos One : Esr Study of Interfacial Hydration Layers of Polypeptides in Water-filled Nanochannels and in Vitrified Bulk Solvents, Volume 8

By Roccatano, Danilo

Click here to view

Book Id: WPLBN0003947943
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos One : Esr Study of Interfacial Hydration Layers of Polypeptides in Water-filled Nanochannels and in Vitrified Bulk Solvents, Volume 8  
Author: Roccatano, Danilo
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Roccatano, D. (n.d.). Plos One : Esr Study of Interfacial Hydration Layers of Polypeptides in Water-filled Nanochannels and in Vitrified Bulk Solvents, Volume 8. Retrieved from http://netlibrary.net/


Description
Description : There is considerable evidence for the essential role of surface water in protein function and structure. However, it is unclear to what extent the hydration water and protein are coupled and interact with each other. Here, we show by ESR experiments (cw, DEER, ESEEM, and ESE techniques) with spin-labeling and nanoconfinement techniques that the vitrified hydration layers can be evidently recognized in the ESR spectra, providing nanoscale understanding for the biological interfacial water. Two peptides of different secondary structures and lengths are studied in vitrified bulk solvents and in water-filled nanochannels of different pore diameter (6.1,7.6 nm). The existence of surface hydration and bulk shells are demonstrated. Water in the immediate vicinity of the nitroxide label (within the van der Waals contacts, ,0.35 nm) at the water-peptide interface is verified to be non-crystalline at 50 K, and the water accessibility changes little with the nanochannel dimension. Nevertheless, this water accessibility for the nanochannel cases is only half the value for the bulk solvent, even though the peptide structures remain largely the same as those immersed in the bulk solvents. On the other hand, the hydration density in the range of ,2 nm from the nitroxide spin increases substantially with decreasing pore size, as the density for the largest pore size (7.6 nm) is comparable to that for the bulk solvent. The results demonstrate that while the peptides are confined but structurally unaltered in the nanochannels, their surrounding water exhibits density heterogeneity along the peptide surface normal. The causes and implications, especially those involving the interactions between the first hydration water and peptides, of these observations are discussed. Spin-label ESR techniques are proven useful for studying the structure and influences of interfacial hydration.

 

Click To View

Additional Books


  • Plos One : Structural Organization of Ma... (by )
  • Plos One : Complete Genome Sequence of t... (by )
  • Plos One : C-terminal Helical Domains of... (by )
  • Plos One : Giemsa-stained Wet Mount Base... (by )
  • Plos One : Low Prevalence of Pneumocysti... (by )
  • Plos One : Wood Densitometry in 17Th and... (by )
  • Plos One : the Association of Systemic M... (by )
  • Plos One : Single Liver Lobe Repopulatio... (by )
  • Plos One : Prion Peptide Uptake in Micro... (by )
  • Plos One : Disability Mediates the Impac... (by )
  • Plos One : Reconstruction of the Transmi... (by )
  • Plos One : Genetic Diversity and Lack of... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.