| 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 |
Related Documents
:
|
7523187 - On the origin of the genetic code. 16862457 - Determination of primary structure of two isoforms 6-1 and 6-2 pla2 d49 from bothrops j... 1576157 - Extracellular lipase from pseudomonas aeruginosa is an amphiphilic protein. 11117877 - Cloning and expression of homospermidine synthase from senecio vulgaris: a revision. 11539447 - The use of gel electrophoresis to study the reactions of activated amino acids with oli... 16601817 - Antimutagenic effect of phenolic acids. |
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. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| 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
Previous Document: Development and validation of an immunochromatographic assay for rapid detection of sulfadiazine in ...
Next Document: Dietary supplements in a national survey: Prevalence of use and reports of adverse events.