Review: Protein design - Where we were, where we are, where we're going

Citation
N. Pokala et Tm. Handel, Review: Protein design - Where we were, where we are, where we're going, J STRUCT B, 134(2-3), 2001, pp. 269-281
Citations number
109
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF STRUCTURAL BIOLOGY
ISSN journal
10478477 → ACNP
Volume
134
Issue
2-3
Year of publication
2001
Pages
269 - 281
Database
ISI
SICI code
1047-8477(200105/06)134:2-3<269:RPD-WW>2.0.ZU;2-8
Abstract
Protein design has become a powerful approach for understanding the relatio nship between amino acid sequence and 3-dimensional structure. In the past 5 years, there have been many breakthroughs in the development of computati onal methods that allow the selection of novel sequences given the structur e of a protein backbone. Successful design of protein scaffolds has now pav ed the way for new endeavors to design function. The. ability to design seq uences compatible with a fold may also be useful in structural and function al genomics by expanding the range of proteins used for fold recognition an d for the identification of functionally important domains from multiple se quence alignments. (C) 2001 Academic Press.