Homology modeling of unknown proteins is based on the assumption that highly similar sequences are likely to share the same fold. However, this does not provide any information on the stability of a given fold, which is ultimately determined by the subtle interplay of enthalpic and entropic contributions. Herein it is shown that ab initio atomistic simulations can be used to predict the effect of point mutations on the stability of a protein fold
Predicting the effect of a point mutation on a protein fold: The villin and advillin headpieces and their Pro62Ala mutants / S., Piana; Laio, Alessandro; F., Marinelli; Troys, ; VAN D., Bourry; C., Ampe; Jc, Martins. - In: JOURNAL OF MOLECULAR BIOLOGY. - ISSN 1089-8638. - 375:2(2008), pp. 460-470. [10.1016/j.jmb.2007.10.020]
Predicting the effect of a point mutation on a protein fold: The villin and advillin headpieces and their Pro62Ala mutants
Laio, Alessandro;
2008-01-01
Abstract
Homology modeling of unknown proteins is based on the assumption that highly similar sequences are likely to share the same fold. However, this does not provide any information on the stability of a given fold, which is ultimately determined by the subtle interplay of enthalpic and entropic contributions. Herein it is shown that ab initio atomistic simulations can be used to predict the effect of point mutations on the stability of a protein foldI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
