Document Detail


Hydrodynamically coupled water in surface adsorbed amino acids as a tool to study hydrated peptides.
MedLine Citation:
PMID:  17126617     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The influence of different amino acid residues on properties of a protein surface is of great interest and importance. Hydrodynamically coupled water in the amino acids has the potential to be used as a tool to study surface properties of proteins. The contribution of this coupled water fraction in design of a hydropathy scale in surface adsorbed amino acid films on solid using quartz crystal microbalance is presented in this work. This scale compares well with the hydropathy scale of Guy reported in the literature and can be correlated with the solid/liquid interfacial tension and work of adhesion of the adsorbed amino acid films. Using Graphical Representation and Analysis of Surface Properties (GRASP) the free energy of transfer from Octanol to water for the amino acids has been estimated and shows approximately an inverse relationship with the coupled water fraction. This scale has been applied in a benchmark test for a native Laminin peptide YIGSR and its mutated sequences (with mutations carried out at 'Y and 'R' positions). The experimentally measured coupled water fractions seem to compare well with that obtained from the present scale assuming the total solvent fraction to be a linear function of the amino acids in the sequence. A survey of the protein data bank showed that sets of sequences based on this scale occur in membrane insertion domain or in trans-membrane proteins suggesting that the scale is suitable to study structure-function correlation in proteins.
Authors:
Muthuselvi Lakshmanan; Aruna Dhathathreyan
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-10-18
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1774     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2007 Jan 
Date Detail:
Created Date:  2007-01-12     Completed Date:  2007-03-23     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  138-45     Citation Subset:  IM    
Affiliation:
Chemical Lab., CLRI, Adyar, Chennai 600 020, India.
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MeSH Terms
Descriptor/Qualifier:
Adsorption
Amino Acid Sequence
Amino Acids / chemistry*
Hydrophobicity
Laminin / chemistry
Peptides / chemistry*
Sequence Alignment
Surface Properties
Thermodynamics
Water / chemistry*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Laminin; 0/Peptides; 7732-18-5/Water

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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