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- W1987348586 abstract "It is a general notion that proteins with very similar three-dimensional structures would show very similar folding kinetics. However, recent studies reveal that the folding kinetic properties of some proteins contradict this thought (i.e., the members in a same protein family fold through different pathways). For example, it has been reported that some beta-proteins in the intracellular lipid-binding protein family fold through quite different pathways (Burns et al., Proteins 1998;33:107-118). Similar differences in folding kinetics are also observed in the members of the globin family (Nishimura et al., Nat Struct Biol 2000;7:679-686). In our study, we examine the possibility of predicting qualitative differences in folding kinetics of the intracellular lipid-binding proteins and two globin proteins (i.e., myoglobin and leghemoglobin). The problem is tackled by means of a contact map based on the average distance statistics between residues, the Average Distance Map (ADM), as constructed from sequence. The ADMs for the three proteins show overall similarity, but some local differences among maps are also observed. Our results demonstrate that some properties of the protein folding kinetics are consistent with local differences in the ADMs. We also discuss the general possibility of predicting folding kinetics from sequence information." @default.
- W1987348586 created "2016-06-24" @default.
- W1987348586 creator A5061553906 @default.
- W1987348586 creator A5079268296 @default.
- W1987348586 date "2003-04-22" @default.
- W1987348586 modified "2023-10-17" @default.
- W1987348586 title "Analysis of the differences in the folding kinetics of structurally homologous proteins based on predictions of the gross features of residue contacts" @default.
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- W1987348586 doi "https://doi.org/10.1002/prot.10378" @default.
- W1987348586 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12784211" @default.
- W1987348586 hasPublicationYear "2003" @default.
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