Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-3-15
pubmed:abstractText
Infrared/UV hole-burning spectroscopy is performed on individual conformers of the protected dipeptide Z-Aib-Pro-NHMe. The extended IR range probed in this study allows one to elucidate both the H-bonding motif (5-7 microm) as well as the backbone structure (7-10 microm). Comparison with DFT calculations shows that the backbone is locally constrained to an alpha-conformation by Aib and to a gamma-turn by Pro. The gamma-turn motif observed here is intriguing since the condensed phase structure is known to be a beta-turn. This is the first actual observation of such a discrepancy, and it emphasizes the subtle balance between intra- and intermolecular forces, which is responsible for the relative stability of the different secondary structure motifs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
128
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3592-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Mid-infrared spectroscopy of protected peptides in the gas phase: a probe of the backbone conformation.
pubmed:affiliation
FOM Institute for Plasma Physics Rijnhuizen, Edisonbaan 14, NL-3439 MN Nieuwegein, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't