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Why are proteins marginally stable?
Taverna DM, Goldstein RA. Taverna DM, et al. Among authors: goldstein ra. Proteins. 2002 Jan 1;46(1):105-9. doi: 10.1002/prot.10016. Proteins. 2002. PMID: 11746707 Free article.
Why are proteins so robust to site mutations?
Taverna DM, Goldstein RA. Taverna DM, et al. Among authors: goldstein ra. J Mol Biol. 2002 Jan 18;315(3):479-84. doi: 10.1006/jmbi.2001.5226. J Mol Biol. 2002. PMID: 11786027
The distribution of structures in evolving protein populations.
Taverna DM, Goldstein RA. Taverna DM, et al. Among authors: goldstein ra. Biopolymers. 2000 Jan;53(1):1-8. doi: 10.1002/(SICI)1097-0282(200001)53:1<1::AID-BIP1>3.0.CO;2-X. Biopolymers. 2000. PMID: 10644946 Free article.
Optimal local propensities for model proteins.
Govindarajan S, Goldstein RA. Govindarajan S, et al. Among authors: goldstein ra. Proteins. 1995 Aug;22(4):413-8. doi: 10.1002/prot.340220411. Proteins. 1995. PMID: 7479714 Free article.
Evolution of model proteins on a foldability landscape.
Govindarajan S, Goldstein RA. Govindarajan S, et al. Among authors: goldstein ra. Proteins. 1997 Dec;29(4):461-6. doi: 10.1002/(sici)1097-0134(199712)29:4<461::aid-prot6>3.0.co;2-b. Proteins. 1997. PMID: 9408943 Free article.
Estimating the total number of protein folds.
Govindarajan S, Recabarren R, Goldstein RA. Govindarajan S, et al. Among authors: goldstein ra. Proteins. 1999 Jun 1;35(4):408-14. Proteins. 1999. PMID: 10382668 Free article.
Why are some proteins structures so common?
Govindarajan S, Goldstein RA. Govindarajan S, et al. Among authors: goldstein ra. Proc Natl Acad Sci U S A. 1996 Apr 16;93(8):3341-5. doi: 10.1073/pnas.93.8.3341. Proc Natl Acad Sci U S A. 1996. PMID: 8622938 Free PMC article.
222 results