Tolerance of a protein helix to multiple alanine and valine substitutions.


Abstract

Protein stability is influenced by the intrinsic secondary structure propensities of the amino acids and by tertiary interactions, but which of these factors dominates is not known in most cases. We have used combinatorial mutagenesis to examine the effects of substituting a good helix-forming residue (alanine) and a poor helix-forming residue (valine) at many positions in an alpha helix of a native protein. This has allowed us to average over many molecular environments and assess to what extent the results reflect intrinsic helical propensities or are masked by tertiary effects. Study holds ProTherm entries: 3167, 3168, 3169, 3170, 3171, 3172, 3173, 3174, 3175, 3176, 3177, 3178, 3179 Extra Details: combinatorial mutagenesis; helix propensity; protein stability;,secondary structure

Submission Details

ID: U2zsbibW4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:21 p.m.

Version: 1

Publication Details
Gregoret LM;Sauer RT,Fold Des (1998) Tolerance of a protein helix to multiple alanine and valine substitutions. PMID:9565756
Additional Information

Sequence Assay Result Units