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.

Protein structure prediction and design

Morea V;
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.
1998
Inglese
177
214
978-0-444-53226-8
http://www.scopus.com/inward/record.url?eid=2-s2.0-0032240054&partnerID=40&md5=bdf22bf057fc86e69c38a72e89c31b79
ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
AMSTERDAM
PAESI BASSI
Sì, ma tipo non specificato
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
4
02 Contributo in Volume::02.01 Contributo in volume (Capitolo o Saggio)
268
none
Morea, V; Leplae, R; Tramontano, ; A,
info:eu-repo/semantics/bookPart
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/199220
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