Conformation dependence of the C Α D Α stretch mode in peptides. II. Explicitly hydrated alanine peptide structures
dc.contributor.author | Mirkin, Noemi G. | en_US |
dc.contributor.author | Krimm, Samuel | en_US |
dc.date.accessioned | 2009-08-12T15:36:27Z | |
dc.date.available | 2010-11-01T15:35:48Z | en_US |
dc.date.issued | 2009-09 | en_US |
dc.identifier.citation | Mirkin, Noemi G.; Krimm, Samuel (2009). "Conformation dependence of the C Α D Α stretch mode in peptides. II. Explicitly hydrated alanine peptide structures." Biopolymers 91(9): 791-800. <http://hdl.handle.net/2027.42/63559> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/63559 | |
dc.description.abstract | Our previous studies of the potential utility of the C Α D Α stretch frequency, Ν(CD), as a tool for determining conformation in peptide systems (Mirkin and Krimm, J Phys Chem A 2004, 108, 10923–10924; 2007, 111, 5300–5303) dealt with the spectroscopic characteristics of isolated alanine peptides with Α R , Β, and polyproline II structures. We have now extended these ab initio calculations to include various explicit-water environments interacting with such conformers. We find that the structure-discriminating feature of this technique is in fact enhanced as a result of the conformation-specific interactions of the bonding waters, in part due to our finding (Mirkin and Krimm, J Phys Chem B 2008, 112, 15268) that C Α [bond]D Α …O(water) hydrogen bonds can be present in addition to those expected between water and the CO and NH of the peptide groups. In fact, Ν(CD) is hardly affected by the latter bonding but can be shifted by up to 70 cm −1 by the former hydrogen bonds. We also discuss the factors that will have to be considered in developing the molecular dynamics (MD) treatment needed to satisfactorily take account of the influence of outer water layers on the structure of the first-layer water molecules that hydrogen bond to the peptide backbone. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 791–800, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com | en_US |
dc.format.extent | 587218 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Polymer and Materials Science | en_US |
dc.title | Conformation dependence of the C Α D Α stretch mode in peptides. II. Explicitly hydrated alanine peptide structures | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | LSA Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055 | en_US |
dc.contributor.affiliationum | LSA Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055 ; LSA Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055 | en_US |
dc.identifier.pmid | 19425050 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/63559/1/21250_ftp.pdf | |
dc.identifier.doi | 10.1002/bip.21250 | en_US |
dc.identifier.source | Biopolymers | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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