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PMID: 9714155 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Protein folding mechanisms and the multidimensional folding funnel.

Proteins ·Vol. 32 ·No. 2 ·1998-08-01 ·Pages 136-58

Socci ND, Onuchic JN, Wolynes PG

Abstract

An important idea that emerges from the energy landscape theory of protein folding is that subtle global features of the protein landscape can profoundly affect the apparent mechanism of folding. The relationship between various characteristic temperatures in the phase diagrams and landmarks in the folding funnel at fixed temperatures can be used to classify different folding behaviors. The one-dimensional picture of a folding funnel classifies folding kinetics into four basic scenarios, depending on the relative location of the thermodynamic barrier and the glass transition as a function of a single-order parameter. However, the folding mechanism may not always be quantitatively described by a single-order parameter. Several other order parameters, such as degree of secondary structure formation, collapse and topological order, are needed to establish the connection between minimalist models and proteins in the laboratory. In this article we describe a simple multidimensional funnel based on two-order parameters that measure the degree of collapse and topological order. The appearance of several different "mechanisms" is illustrated by analyzing lattice models with different potentials and sequences with different degrees of design. In most cases, the two-dimensional analysis leads to a classification of mechanisms totally in keeping with the one-dimensional scheme, but a topologically distinct scenario of fast folding with traps also emerges. The nature of traps depends on the relative location of the glass transition surface and the thermodynamic barrier in the multidimensional funnel.

MeSH Terms
Computer Simulation Entropy Kinetics Mathematical Computing Models, Chemical Monte Carlo Method Probability Protein Conformation Protein Folding Protein Structure, Secondary Temperature
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Socci N D
Bell Laboratories, Lucent Technologies, Murray Hill, New Jersey 07974, USA.
Onuchic J N
Wolynes P G
Article Info
Journal
Proteins
Abbr.
Proteins
ISSN
0887-3585
Published
1998-08-01
Pages
136-58
Language
English
Region
United States
NLM ID
8700181
Subset
IM
Grants
NIGMS NIH HHS · 1R01 GM44557 · United States
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