An expanded view of the protein folding landscape of PDZ domains

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

An expanded view of the protein folding landscape of PDZ domains. / Hultqvist, Greta; Pedersen, Søren W; Chi, Celestine N.; Strømgaard, Kristian; Gianni, Stefano; Jemth, Per.

I: Biochemical and Biophysical Research Communications, Bind 421, Nr. 3, 11.05.2012, s. 550-553.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Hultqvist, G, Pedersen, SW, Chi, CN, Strømgaard, K, Gianni, S & Jemth, P 2012, 'An expanded view of the protein folding landscape of PDZ domains', Biochemical and Biophysical Research Communications, bind 421, nr. 3, s. 550-553. https://doi.org/10.1016/j.bbrc.2012.04.042

APA

Hultqvist, G., Pedersen, S. W., Chi, C. N., Strømgaard, K., Gianni, S., & Jemth, P. (2012). An expanded view of the protein folding landscape of PDZ domains. Biochemical and Biophysical Research Communications, 421(3), 550-553. https://doi.org/10.1016/j.bbrc.2012.04.042

Vancouver

Hultqvist G, Pedersen SW, Chi CN, Strømgaard K, Gianni S, Jemth P. An expanded view of the protein folding landscape of PDZ domains. Biochemical and Biophysical Research Communications. 2012 maj 11;421(3):550-553. https://doi.org/10.1016/j.bbrc.2012.04.042

Author

Hultqvist, Greta ; Pedersen, Søren W ; Chi, Celestine N. ; Strømgaard, Kristian ; Gianni, Stefano ; Jemth, Per. / An expanded view of the protein folding landscape of PDZ domains. I: Biochemical and Biophysical Research Communications. 2012 ; Bind 421, Nr. 3. s. 550-553.

Bibtex

@article{a38fb31f2f404ddeaa4a7efe56b17547,

title = "An expanded view of the protein folding landscape of PDZ domains",

abstract = "Most protein domains fold in an apparently co-operative and two-state manner with only the native and denatured states significantly populated at any experimental condition. However, the protein folding energy landscape is often rugged and different transition states may be rate limiting for the folding reaction under different conditions, as seen for the PDZ protein domain family. We have here analyzed the folding kinetics of two PDZ domains and found that a previously undetected third transition state is rate limiting under conditions that stabilize the native state relative to the denatured state. In light of these results, we have re-analyzed previous folding data on PDZ domains and present a unified folding mechanism with three distinct transition states separated by two high-energy intermediates. Our data show that sequence composition tunes the relative stabilities of folding transition states within the PDZ family, while the overall mechanism is determined by topology. This model captures the kinetic folding mechanism of all PDZ domains studied to date.",

keywords = "Kinetics, Models, Chemical, Mutation, PDZ Domains, Protein Folding",

author = "Greta Hultqvist and Pedersen, {S{\o}ren W} and Chi, {Celestine N.} and Kristian Str{\o}mgaard and Stefano Gianni and Per Jemth",

year = "2012",

month = may,

day = "11",

doi = "10.1016/j.bbrc.2012.04.042",

language = "English",

volume = "421",

pages = "550--553",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "3",

}

RIS

TY - JOUR

T1 - An expanded view of the protein folding landscape of PDZ domains

AU - Hultqvist, Greta

AU - Pedersen, Søren W

AU - Chi, Celestine N.

AU - Strømgaard, Kristian

AU - Gianni, Stefano

AU - Jemth, Per

PY - 2012/5/11

Y1 - 2012/5/11

N2 - Most protein domains fold in an apparently co-operative and two-state manner with only the native and denatured states significantly populated at any experimental condition. However, the protein folding energy landscape is often rugged and different transition states may be rate limiting for the folding reaction under different conditions, as seen for the PDZ protein domain family. We have here analyzed the folding kinetics of two PDZ domains and found that a previously undetected third transition state is rate limiting under conditions that stabilize the native state relative to the denatured state. In light of these results, we have re-analyzed previous folding data on PDZ domains and present a unified folding mechanism with three distinct transition states separated by two high-energy intermediates. Our data show that sequence composition tunes the relative stabilities of folding transition states within the PDZ family, while the overall mechanism is determined by topology. This model captures the kinetic folding mechanism of all PDZ domains studied to date.

AB - Most protein domains fold in an apparently co-operative and two-state manner with only the native and denatured states significantly populated at any experimental condition. However, the protein folding energy landscape is often rugged and different transition states may be rate limiting for the folding reaction under different conditions, as seen for the PDZ protein domain family. We have here analyzed the folding kinetics of two PDZ domains and found that a previously undetected third transition state is rate limiting under conditions that stabilize the native state relative to the denatured state. In light of these results, we have re-analyzed previous folding data on PDZ domains and present a unified folding mechanism with three distinct transition states separated by two high-energy intermediates. Our data show that sequence composition tunes the relative stabilities of folding transition states within the PDZ family, while the overall mechanism is determined by topology. This model captures the kinetic folding mechanism of all PDZ domains studied to date.

KW - Kinetics

KW - Models, Chemical

KW - Mutation

KW - PDZ Domains

KW - Protein Folding

U2 - 10.1016/j.bbrc.2012.04.042

DO - 10.1016/j.bbrc.2012.04.042

M3 - Journal article

C2 - 22521641

VL - 421

SP - 550

EP - 553

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

ID: 45807323