K
Kathleen G. Valentine
Researcher at University of Pennsylvania
Publications - 53
Citations - 2801
Kathleen G. Valentine is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Micelle. The author has an hindex of 29, co-authored 52 publications receiving 2598 citations. Previous affiliations of Kathleen G. Valentine include University of Maryland Biotechnology Institute.
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Journal ArticleDOI
Conformational entropy in molecular recognition by proteins
TL;DR: It is found that the change in internal dynamics of the protein calmodulin varies significantly on binding a variety of target domains, indicating that changes in protein conformational entropy can contribute significantly to the free energy of protein–ligand association.
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The role of conformational entropy in molecular recognition by calmodulin
TL;DR: An “entropy meter” is calibrated employing an experimental dynamical proxy based on NMR relaxation and it is shown that changes in the conformational entropy of calmodulin are a significant component of the energetics of binding and the distribution of motion at the interface between the target domain and cal modulin are surprisingly non-complementary.
Journal ArticleDOI
Protein structure by solid-state NMR spectroscopy.
TL;DR: Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution.
Journal ArticleDOI
Entropy in molecular recognition by proteins.
Jose A. Caro,Kyle W. Harpole,Vignesh Kasinath,Jackwee Lim,Jeffrey M. Granja,Kathleen G. Valentine,Kim A. Sharp,A. Joshua Wand +7 more
TL;DR: A comprehensive and unified view of the general role of entropy in high-affinity molecular recognition by proteins is provided using a dynamical proxy provided by NMR relaxation methods that finds that conformational entropy can contribute significantly and variably to the thermodynamics of binding.
Journal ArticleDOI
Elementary tetrahelical protein design for diverse oxidoreductase functions
Tammer A. Farid,Goutham Kodali,Lee A. Solomon,Bruce R. Lichtenstein,Bruce R. Lichtenstein,Molly M. Sheehan,Bryan A. Fry,Chris Bialas,Nathan M. Ennist,Jessica A Siedlecki,Zhenyu Zhao,Matthew A. Stetz,Kathleen G. Valentine,J. L. Ross Anderson,A. Joshua Wand,Bohdana M. Discher,Christopher C. Moser,P. Leslie Dutton +17 more
TL;DR: A man-made protein platform that reproduces many of the diverse functions of natural oxidoreductases without importing the complex and obscure interactions common to natural proteins is described.