R
Robert H. Kretsinger
Researcher at University of Virginia
Publications - 112
Citations - 7647
Robert H. Kretsinger is an academic researcher from University of Virginia. The author has contributed to research in topics: Calmodulin & Protein structure. The author has an hindex of 39, co-authored 110 publications receiving 7421 citations. Previous affiliations of Robert H. Kretsinger include Yokohama City University.
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Carp Muscle Calcium-binding Protein II. STRUCTURE DETERMINATION AND GENERAL DESCRIPTION
TL;DR: The structure of crystalline carp muscle calcium-binding protein (parvalbumin) has been determined by x-ray diffraction techniques to nominal 1.85-A resolution and the electron density map is interpreted in terms of the 108 amino acid sequence described in Paper I in this series.
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Structure and evolution of calcium-modulated proteins.
TL;DR: The intracellular functions of calcium are best understood in terms of calcium's functioning as a second messenger, and this line of thought leads to a suggestion of the evolutionary reason for the choice of calcium as the sole inorganic second messenger.
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Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysis
P.C. Moews,Robert H. Kretsinger +1 more
TL;DR: The structure of carp muscle calcium-binding parvalbumin has been refined to an overall residual of 0.25 by a combination of model building and difference Fourier analyses, and these procedures and results are applicable to other protein refinement problems.
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Classification and evolution of EF-hand proteins
TL;DR: Forty-five distinct subfamilies of EF-hand proteins have been identified; many sequence and chem-ical characteristics do not show systemic trends by subfamily or species of host organisms; such homoplasy is widespread.
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Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme.
TL;DR: A computer search of available protein sequences and structures suggests that bacteriophage T4 lysozyme contains one region and that rabbit myosin light chains contain three regions similar, and supposedly homologous, to the calcium binding region of carp muscle calcium binding parvalbumin.