Protein stability, flexibility and function
Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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Protein stability, flexibility and function. / Teilum, Kaare; Olsen, Johan G; Kragelund, Birthe B.
I: B B A - Proteins and Proteomics, Bind 1814, Nr. 8, 2011, s. 969-76.Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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TY - JOUR
T1 - Protein stability, flexibility and function
AU - Teilum, Kaare
AU - Olsen, Johan G
AU - Kragelund, Birthe B
N1 - Copyright © 2010 Elsevier B.V. All rights reserved.
PY - 2011
Y1 - 2011
N2 - Proteins rely on flexibility to respond to environmental changes, ligand binding and chemical modifications. Potentially, a perturbation that changes the flexibility of a protein may interfere with its function. Millions of mutations have been performed on thousands of proteins in quests for a delineation of the molecular details of their function. Several of these mutations interfered with the binding of a specific ligand with a concomitant effect on the stability of the protein scaffold. It has been ambiguous and not straightforward to recognize if any relationships exist between the stability of a protein and the affinity for its ligand. In this review, we present examples of proteins where changes in stability results in changes in affinity and of proteins where stability and affinity are uncorrelated. We discuss the possibility for a relationship between stability and binding. From the data presented is it clear that there are specific sites (flexibility hotspots) in proteins that are important for both binding and stability. This article is part of a Special Issue entitled: Protein Dynamics: Experimental and Computational Approaches.
AB - Proteins rely on flexibility to respond to environmental changes, ligand binding and chemical modifications. Potentially, a perturbation that changes the flexibility of a protein may interfere with its function. Millions of mutations have been performed on thousands of proteins in quests for a delineation of the molecular details of their function. Several of these mutations interfered with the binding of a specific ligand with a concomitant effect on the stability of the protein scaffold. It has been ambiguous and not straightforward to recognize if any relationships exist between the stability of a protein and the affinity for its ligand. In this review, we present examples of proteins where changes in stability results in changes in affinity and of proteins where stability and affinity are uncorrelated. We discuss the possibility for a relationship between stability and binding. From the data presented is it clear that there are specific sites (flexibility hotspots) in proteins that are important for both binding and stability. This article is part of a Special Issue entitled: Protein Dynamics: Experimental and Computational Approaches.
U2 - 10.1016/j.bbapap.2010.11.005
DO - 10.1016/j.bbapap.2010.11.005
M3 - Review
C2 - 21094283
VL - 1814
SP - 969
EP - 976
JO - B B A - Proteins and Proteomics
JF - B B A - Proteins and Proteomics
SN - 1570-9639
IS - 8
ER -
ID: 33682271