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| Title: | Conformational changes of peptides at solid/liquid interfaces: A Monte Carlo study |
| Author (s): | Mungikar, Amol A. Forciniti, Daniel |
| Department/Lab Affiliations: | Center for Environmental Science and Technology (CEST) Chemical & Biological Engineering |
| Keywords: | aspartic acid diblock units hydrophobic dehydration |
| Subject Terms: | Peptides. |
| Issue Date: | 2004-09-25 |
| Publisher: | American Chemical Society |
| Citation: | Mungikar, Amol A., and Forciniti, Daniel. "Conformational Changes of Peptides at Solid/Liquid Interfaces: A Monte Carlo Study." Biomacromolecules, vol. 5, no. 6, 2004. |
| Abstract: | Monte Carlo simulations were performed to study the conformational changes of negatively charged model peptides dissolved in water adsorbed onto charged surfaces. 8-, 16-, and 20-residues peptides were used, each of them consisted of repeating diblock units of aspartic acid (ASP, polar amino acid) and isoleucine (ILE, nonpolar amino acid) residues. We found that a water patch was retained at the charged surface, separating the peptide from it. We believed that these water molecules were primarily responsible for giving a particular orientation to the peptide at the surface. Water did play a role to some extent in the structural stability of the 8-residues peptide. However, for higher chain lengths (16-residues and 20-residues), the intrinsic hydrogen-bonding network (or intrinsic structural stability) showed a predominant effect over hydrophobic dehydration for the stability of the peptide at the surface. |
| Type: | Article - Journal text |
| In Title: | Biomacromolecules |
| Copyright Notice: | This material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder. FULL COPYRIGHT INFORMATION: |
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| title | Conformational changes of peptides at solid/liquid interfaces: A Monte Carlo study |
| contributor.author | Mungikar, Amol A. |
| contributor.author | Forciniti, Daniel |
| contributor.deptlab | Center for Environmental Science and Technology (CEST) |
| contributor.deptlab | Chemical & Biological Engineering |
| contributor.sponsor | National Science Foundation |
| subject | aspartic acid |
| subject | diblock units |
| subject | hydrophobic dehydration |
| subject.LCSH | Peptides. |
| date.issued | 2004-09-25 |
| publisher | American Chemical Society |
| identifier.citation | Mungikar, Amol A., and Forciniti, Daniel. "Conformational Changes of Peptides at Solid/Liquid Interfaces: A Monte Carlo Study." Biomacromolecules, vol. 5, no. 6, 2004. |
| identifier.pub.URI | |
| description.abstract | Monte Carlo simulations were performed to study the conformational changes of negatively charged model peptides dissolved in water adsorbed onto charged surfaces. 8-, 16-, and 20-residues peptides were used, each of them consisted of repeating diblock units of aspartic acid (ASP, polar amino acid) and isoleucine (ILE, nonpolar amino acid) residues. We found that a water patch was retained at the charged surface, separating the peptide from it. We believed that these water molecules were primarily responsible for giving a particular orientation to the peptide at the surface. Water did play a role to some extent in the structural stability of the 8-residues peptide. However, for higher chain lengths (16-residues and 20-residues), the intrinsic hydrogen-bonding network (or intrinsic structural stability) showed a predominant effect over hydrophobic dehydration for the stability of the peptide at the surface. |
| type | Article - Journal |
| type.DCMIType | text |
| type.status | Final version |
| rights | This material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder. |
| rights.URI | |
| relation.isPartOf | Biomacromolecules |
| date.accessioned | 2008-05-20T19:02:08Z |
| date.available | 2008-05-30T19:12:32Z |
| identifier.persist.URI |