WFRF:(Ardell David H)
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03243naa a2200433 4500 | |
| 001 | oai:DiVA.org:uu-127461 | |
| 003 | SwePub | |
| 008 | 100713s2009 | |||||||||||000 ||eng| | |
| 009 | oai:DiVA.org:su-34574 | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1274612 URI |
| 024 | 7 | a https://doi.org/10.1002/prot.224582 DOI |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-345742 URI |
| 040 | a (SwePub)uud (SwePub)su | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Illergård, Kristofferu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)kille |
| 245 | 1 0 | a Structure is three to ten times more conserved than sequence-A study of structural response in protein cores |
| 264 | 1 | b Wiley,c 2009 |
| 338 | a print2 rdacarrier | |
| 520 | a 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. | |
| 650 | 7 | a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng |
| 653 | a protein structure | |
| 653 | a evolution | |
| 653 | a secondary structure | |
| 653 | a accessibility | |
| 653 | a residue contacts | |
| 653 | a RMSD | |
| 653 | a Biology | |
| 653 | a Biologi | |
| 700 | 1 | a Ardell, David H.u Uppsala universitet,Centrum för bioinformatik4 aut |
| 700 | 1 | a Elofsson, Arneu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)aelof |
| 710 | 2 | a Stockholms universitetb Institutionen för biokemi och biofysik4 org |
| 773 | 0 | t Proteinsd : Wileyg 77:3, s. 499-508q 77:3<499-508x 0887-3585x 1097-0134 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-127461 |
| 856 | 4 8 | u https://doi.org/10.1002/prot.22458 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-34574 |
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