The preferred conformation of dipeptides in the context of biosynthesis
Bywater, Robert P. and Veryazov, Valera LU
(2013)
In Naturwissenschaften
100(9).
p.853-859
- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4062377
- author
- Bywater, Robert P.
and Veryazov, Valera
LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Dipeptides, Biosynthesis, Proteins
- in
- Naturwissenschaften
- volume
- 100
- issue
- 9
- pages
- 853 - 859
- publisher
- Springer
- external identifiers
-
- wos:000323670800005
- scopus:84883456355
- pmid:23942479
- ISSN
- 1432-1904
- DOI
- 10.1007/s00114-013-1085-7
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- b7035b53-671f-4426-9d9a-4f4776585e5d (old id 4062377)
- date added to LUP
- 2016-04-01 14:50:52
- date last changed
- 2023-01-04 07:10:02
@article{b7035b53-671f-4426-9d9a-4f4776585e5d,
abstract = {{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.}},
author = {{Bywater, Robert P. and Veryazov, Valera}},
issn = {{1432-1904}},
keywords = {{Dipeptides; Biosynthesis; Proteins}},
language = {{eng}},
number = {{9}},
pages = {{853--859}},
publisher = {{Springer}},
series = {{Naturwissenschaften}},
title = {{The preferred conformation of dipeptides in the context of biosynthesis}},
url = {{http://dx.doi.org/10.1007/s00114-013-1085-7}},
doi = {{10.1007/s00114-013-1085-7}},
volume = {{100}},
year = {{2013}},
}