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1c3t
From Proteopedia
| 1c3t, 20 NMR models () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
ROTAMER STRAIN AS A DETERMINANT OF PROTEIN STRUCTURAL SPECIFICITY
We present direct evidence for a change in protein structural specificity due to hydrophobic core packing. High resolution structural analysis of a designed core variant of ubiquitin reveals that the protein is in slow exchange between two conformations. Examination of side-chain rotamers indicates that this dynamic response and the lower stability of the protein are coupled to greater strain and mobility in the core. The results suggest that manipulating the level of side-chain strain may be one way of fine tuning the stability and specificity of proteins.
Rotamer strain as a determinant of protein structural specificity., Lazar GA, Johnson EC, Desjarlais JR, Handel TM, Protein Sci. 1999 Dec;8(12):2598-610. PMID:10631975
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1c3t is a 1 chain structure of Ubiquitin with sequence from Homo sapiens. Full experimental information is available from OCA.
See Also
Reference
- Lazar GA, Johnson EC, Desjarlais JR, Handel TM. Rotamer strain as a determinant of protein structural specificity. Protein Sci. 1999 Dec;8(12):2598-610. PMID:10631975
