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Literature DB >> 10631990

Robustness of protein folding kinetics to surface hydrophobic substitutions.

H Gu¹, N Doshi, D E Kim, K T Simons, J V Santiago, S Nauli, D Baker.

Abstract

We use both combinatorial and site-directed mutagenesis to explore the consequences of surface hydrophobic substitutions for the folding of two small single domain proteins, the src SH3 domain, and the IgG binding domain of Peptostreptococcal protein L. We find that in almost every case, destabilizing surface hydrophobic substitutions have much larger effects on the rate of unfolding than on the rate of folding, suggesting that nonnative hydrophobic interactions do not significantly interfere with the rate of core assembly.

Entities: Gene

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Year: 1999 PMID： 10631990 PMCID： PMC2144221 DOI： 10.1110/ps.8.12.2734

Source DB: PubMed Journal: Protein Sci ISSN： 0961-8368 Impact factor: 6.725

20 in total

Robustness of protein folding kinetics to surface hydrophobic substitutions.

1. Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures.

2. A phage display system for studying the sequence determinants of protein folding.

3. Guidelines for protein design: the energetics of beta sheet side chain interactions.

Review 4. Principles of protein folding--a perspective from simple exact models.

5. Initial hydrophobic collapse in the folding of barstar.

6. Amino-acid substitutions in a surface turn modulate protein stability.

7. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins.

8. The hydrophobic moment detects periodicity in protein hydrophobicity.

9. Molecular collapse: the rate-limiting step in two-state cytochrome c folding.

10. Kinetics of folding of the IgG binding domain of peptostreptococcal protein L.

1. Unspecific hydrophobic stabilization of folding transition states.

Review 2. Genomic biodiversity, phylogenetics and coevolution in proteins.

3. Protein folding is mechanistically robust.

4. Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis.

5. Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustness.

6. Biophysics of protein evolution and evolutionary protein biophysics.

7. Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.

8. Modulation of contact order effects in the two-state folding of stefins A and B.