Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 41, Pages 31095-31099Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R110.157685
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Funding
- NCRR NIH HHS [R00 RR024107-04, K99 RR024107, R00 RR024107-03, R00 RR024107, K99 RR024107-01A1, R00 RR024107-02] Funding Source: Medline
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A long-standing goal of computational protein design is to create proteins similar to those found in Nature. One motivation is to harness the exquisite functional capabilities of proteins for our own purposes. The extent of similarity between designed and natural proteins also reports on how faithfully our models represent the selective pressures that determine protein sequences. As the field of protein design shifts emphasis from reproducing native-like protein structure to function, it has become important that these models treat the notion of specificity in molecular interactions. Although specificity may, in some cases, be achieved by optimization of a desired protein in isolation, methods have been developed to address directly the desire for proteins that exhibit specific functions and interactions.
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