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Protein structure prediction and design

Capitolo di libro
Data di Pubblicazione:
1998
Abstract:
Proteins have a unique native conformation, which can be proven in many instances to be determined by the amino acid sequence alone. The folding problem, that is the understanding of how the amino acid sequence directs folding, is still unsolved, despite more than 30 years of effort. However, many new methods have appeared in the past few years. This chapter describes the different principles underlying them and tries to give an overview of their successes and pitfalls.
Tipologia CRIS:
02.01 Contributo in volume (Capitolo o Saggio)
Keywords:
ab initio methods; CASP; comparative modelling; energy function; fold recognition; force field; long-range interactions; loop; modelling by homology; multiple sequence alignmen; protein design; protein folds; residue conservation; rotamer; secondary structure prediction; sequence alignment; sequence pattern; side chains; structure prediction; threading
Elenco autori:
Morea, Veronica
Autori di Ateneo:
MOREA VERONICA
Link alla scheda completa:
https://iris.cnr.it/handle/20.500.14243/199220
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http://www.scopus.com/inward/record.url?eid=2-s2.0-0032240054&partnerID=40&md5=bdf22bf057fc86e69c38a72e89c31b79
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