Abstract
Proteins are dynamic entities that exert, in some cases, their functions via complex pathways, involving active transient species. This phenomenon was highlighted for the first time in 1983 by Antonini et al. (J. Biol. Chem. 258, 4676-4678), who demonstrated that at least one intermediate occurring in the formation of the bovine β-trypsin-Kunitz inhibitor complex displayed catalytic properties different from those of the active enzyme and of the inactive enzyme-inhibitor adduct. Since it was impossible to explain this phenomenon in terms of static three-dimensional structures, the term "chronosteric effects" was coined to capture the observation that transient species are relevant to protein function(s). Here, some recent results on the folding and function of proteins are reported on the light of chronosteric effects.
| Original language | English |
|---|---|
| Pages (from-to) | 836-844 |
| Number of pages | 9 |
| Journal | IUBMB Life |
| Volume | 65 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 2013 |
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Keywords
- chronosteric effects
- folding intermediates
- human estrogen receptors
- human serum heme-albumin
- kinetics
- protein folding
- rapid signals and transcription activity
- serine proteinase inhibition
- transient catalytic properties
- transient heme-based reactivity
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Clinical Biochemistry
- Molecular Biology
- Genetics
Cite this
Functional role of transient conformations : Rediscovering "chronosteric effects" thirty years later. / Ascenzi, Paolo; Gianni, Stefano.
In: IUBMB Life, Vol. 65, No. 10, 10.2013, p. 836-844.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Functional role of transient conformations
T2 - Rediscovering "chronosteric effects" thirty years later
AU - Ascenzi, Paolo
AU - Gianni, Stefano
PY - 2013/10
Y1 - 2013/10
N2 - Proteins are dynamic entities that exert, in some cases, their functions via complex pathways, involving active transient species. This phenomenon was highlighted for the first time in 1983 by Antonini et al. (J. Biol. Chem. 258, 4676-4678), who demonstrated that at least one intermediate occurring in the formation of the bovine β-trypsin-Kunitz inhibitor complex displayed catalytic properties different from those of the active enzyme and of the inactive enzyme-inhibitor adduct. Since it was impossible to explain this phenomenon in terms of static three-dimensional structures, the term "chronosteric effects" was coined to capture the observation that transient species are relevant to protein function(s). Here, some recent results on the folding and function of proteins are reported on the light of chronosteric effects.
AB - Proteins are dynamic entities that exert, in some cases, their functions via complex pathways, involving active transient species. This phenomenon was highlighted for the first time in 1983 by Antonini et al. (J. Biol. Chem. 258, 4676-4678), who demonstrated that at least one intermediate occurring in the formation of the bovine β-trypsin-Kunitz inhibitor complex displayed catalytic properties different from those of the active enzyme and of the inactive enzyme-inhibitor adduct. Since it was impossible to explain this phenomenon in terms of static three-dimensional structures, the term "chronosteric effects" was coined to capture the observation that transient species are relevant to protein function(s). Here, some recent results on the folding and function of proteins are reported on the light of chronosteric effects.
KW - chronosteric effects
KW - folding intermediates
KW - human estrogen receptors
KW - human serum heme-albumin
KW - kinetics
KW - protein folding
KW - rapid signals and transcription activity
KW - serine proteinase inhibition
KW - transient catalytic properties
KW - transient heme-based reactivity
UR - http://www.scopus.com/inward/record.url?scp=84884923355&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84884923355&partnerID=8YFLogxK
U2 - 10.1002/iub.1208
DO - 10.1002/iub.1208
M3 - Article
C2 - 24078391
AN - SCOPUS:84884923355
VL - 65
SP - 836
EP - 844
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 10
ER -