1C3T

ROTAMER STRAIN AS A DETERMINANT OF PROTEIN STRUCTURAL SPECIFICITY

Summary for 1C3T

• Entry DOI: 10.2210/pdb1c3t/pdb
• NMR Information: BMRB: 4663
• Descriptor: PROTEIN (1D8 UBIQUITIN) (1 entity in total)
• Functional Keywords: protein design, hydrophobic core, packing, rotamers, roc, ubiquitin, de novo protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8576.83

Authors

Lazar, G.A.,Johnson, E.C.,Desjarlais, J.R.,Handel, T.M. (deposition date: 1999-07-28, release date: 1999-08-20, Last modification date: 2024-04-10)

Primary citation

Lazar, G.A.,Johnson, E.C.,Desjarlais, J.R.,Handel, T.M.
Rotamer strain as a determinant of protein structural specificity.
Protein Sci., 8:2598-2610, 1999

PubMed Abstract: 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.

PubMed: 10631975

Experimental method

SOLUTION NMR