TY - JOUR

T1 - Thermodynamics of proteins

T2 - Fast folders and sharp transitions

AU - Bakk, Audun

AU - Dommersnes, Paul G.

AU - Hansen, Alex

AU - Høye, Johan S.

AU - Sneppen, Kim

AU - Jensen, Mogens H.

PY - 2002/1/1

Y1 - 2002/1/1

N2 - Several small globular proteins exhibit a simple two-state folding process (sharp transition). The rather short folding times of proteins (fast folders) indicate that folding is guided through some sequence of contact bindings. We discuss the possibility for reconciling a two-state folding event with a sequential folding process, i.e. a folding pathway in a schematic model of protein folding. We show that both single and multiple folding pathways can lead to an apparent two-state folding from a thermodynamic point of view. We also discuss water interactions in protein folding, leading to cold and warm destabilization of the protein.

AB - Several small globular proteins exhibit a simple two-state folding process (sharp transition). The rather short folding times of proteins (fast folders) indicate that folding is guided through some sequence of contact bindings. We discuss the possibility for reconciling a two-state folding event with a sequential folding process, i.e. a folding pathway in a schematic model of protein folding. We show that both single and multiple folding pathways can lead to an apparent two-state folding from a thermodynamic point of view. We also discuss water interactions in protein folding, leading to cold and warm destabilization of the protein.

KW - Folding pathway

KW - Protein folding

KW - Thermodynamics

KW - Van't Hoff enthalpy relation

UR - http://www.scopus.com/inward/record.url?scp=0036681493&partnerID=8YFLogxK

U2 - 10.1016/S0010-4655(02)00293-X

DO - 10.1016/S0010-4655(02)00293-X

M3 - Journal article

AN - SCOPUS:0036681493

VL - 147

SP - 307

EP - 312

JO - Computer Physics Communications

JF - Computer Physics Communications

SN - 0010-4655

IS - 1-2

ER -