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The preferred confo...
The preferred conformation of dipeptides in the context of biosynthesis
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Bywater, Robert P. (author)
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- Veryazov, Valera (author)
- Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 2013-08-13
- 2013
- English.
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In: Naturwissenschaften. - : Springer Science and Business Media LLC. - 1432-1904 .- 0028-1042. ; 100:9, s. 853-859
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http://dx.doi.org/10...
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Abstract
Subject headings
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- Globular proteins are folded polypeptide structures comprising stretches of secondary structures (helical (alpha- or 3(10) helix type), polyproline helix or beta-strands) interspersed by regions of less well-ordered structure ("random coil"). Protein fold prediction is a very active field impacting inte alia on protein engineering and misfolding studies. Apart from the many studies of protein refolding from the denatured state, there has been considerable interest in studying the initial formation of peptides during biosynthesis, when there are at the outset only a few residues in the emerging polypeptide. Although there have been many studies employing quantum chemical methods of the conformation of dipeptides, these have mostly been carried out in the gas phase or simulated water. None of these conditions really apply in the interior confines of the ribosome. In the present work, we are concerned with the conformation of dipeptides in this low dielectric environment. Furthermore, only the residue types glycine and alanine have been studied by previous authors, but we extend this repertoire to include leucine and isoleucine, position isomers which have very different structural propensities.
Subject headings
- NATURVETENSKAP -- Kemi -- Teoretisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
Keyword
- Dipeptides
- Biosynthesis
- Proteins
Publication and Content Type
- art (subject category)
- ref (subject category)
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