1H8K: A-SPECTRIN SH3 DOMAIN A11V, V23L, M25V, V53I, V58L MUTANT

Citation:
Abstract
We have designed de novo 13 divergent spectrin SH3 core sequences to determine their folding properties. Kinetic analysis of the variants with stability similar to that of the wild type protein shows accelerated unfolding and refolding rates compatible with a preferential stabilization of the transition state. This is most likely caused by conformational strain in the native state, as deletion of a methyl group (Ile-->Val) leads to deceleration in unfolding and increased stability (up to 2 kcal x mol(-1)). Several of these Ile-->Val mutants have negative phi(-U) values, indicating that some noncanonical phi(-U) values might result from conformational strain. Thus, producing a stable protein does not necessarily mean that the design process has been entirely successful. Strained interactions could have been introduced, and a reduction in the buried volume could result in a large increase in stability and a reduction in unfolding rates.
PDB ID: 1H8KDownload
MMDB ID: 19436
PDB Deposition Date: 2001/2/9
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1H8K: monomeric; determined by author and by software (PQS)
Molecular Components in 1H8K
Label Count Molecule
Protein (1 molecule)
1
Spectrin Alpha Chain(Gene symbol: SPTAN1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.