Search: WFRF:(Ardell David H) >
Structure is three ...
-
Illergård, KristofferStockholms universitet,Institutionen för biokemi och biofysik
(author)
Structure is three to ten times more conserved than sequence-A study of structural response in protein cores
- Article/chapterEnglish2009
Publisher, publication year, extent ...
-
Wiley,2009
-
printrdacarrier
Numbers
-
LIBRIS-ID:oai:DiVA.org:uu-127461
-
https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-127461URI
-
https://doi.org/10.1002/prot.22458DOI
-
https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-34574URI
Supplementary language notes
-
Language:English
-
Summary in:English
Part of subdatabase
Classification
-
Subject category:ref swepub-contenttype
-
Subject category:art swepub-publicationtype
Notes
-
Protein structures change during evolution in response to mutations. Here, we analyze the mapping between sequence and structure in a set of structurally aligned protein domains. To avoid artifacts, we restricted our attention only to the core components of these structures. We found that on average, using different measures of structural change, protein cores evolve linearly with evolutionary distance (amino acid substitutions per site). This is true irrespective of which measure of structural change we used, whether RMSD or discrete structural descriptors for secondary structure, accessibility, or contacts. This linear response allows us to quantify the claim that structure is more conserved than sequence. Using structural alphabets of similar cardinality to the sequence alphabet, structural cores evolve three to ten times slower than sequences. Although we observed an average linear response, we found a wide variance. Different domain families varied fivefold in structural response to evolution. An attempt to categorically analyze this variance among subgroups by structural and functional category revealed only one statistically significant trend. This trend can be explained by the fact that beta-sheets change faster than alpha-helices, most likely due to that they are shorter and that change occurs at the ends of the secondary structure elements. Proteins 2009; 77:499-508. (C) 2009 Wiley-Liss, Inc.
Subject headings and genre
Added entries (persons, corporate bodies, meetings, titles ...)
-
Ardell, David H.Uppsala universitet,Centrum för bioinformatik
(author)
-
Elofsson, ArneStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)aelof
(author)
-
Stockholms universitetInstitutionen för biokemi och biofysik
(creator_code:org_t)
Related titles
-
In:Proteins: Wiley77:3, s. 499-5080887-35851097-0134
Internet link
Find in a library
-
Proteins
(Search for host publication in LIBRIS)
To the university's database