國立虎尾科技大學 |

Protein-ligand binding thermodynamics /

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Protein-ligand binding thermodynamics // Justin M. Miller and Justin D. Marsee.
作者:	Miller, Justin M.,
其他作者:	Marsee, Justin D.,
面頁冊數:	1 online resource :illustrations (some color). :
標題:	Binding free energy. -
電子資源:	http://dx.doi.org/10.1021/acsinfocus.7e7011
ISBN:	9780841299795

Protein-ligand binding thermodynamics /
Miller, Justin M.,

Protein-ligand binding thermodynamics /Justin M. Miller and Justin D. Marsee. - 1 online resource :illustrations (some color). - ACS in focus,2691-8307. - ACS in focus,.

Includes bibliographical references and index.

Introduction --

"Ligand binding by macromolecules represents a core event of broad relevance to a range of systems, including catalytic systems alongside noncatalytic systems such as nucleic acid binding by transcription factors or extracellular ligand binding by proteins involved in signaling pathways. The scope of this primer is constrained to introduce only foundational models without significant discussion of more advanced topics such as allosteric or linkage effects. Linkage occurs when the binding of a ligand is influenced by the binding of another molecule of the same ligand (homotropic linkage), the binding of a different ligand (heterotropic linkage), physical variables such as temperature or pressure (physical linkage), or changes in macromolecular assembly state (polysteric linkage). Taking this into account, the foundational themes presented in this primer can be used to describe any macromolecule-ligand interaction either by direct use of the models and techniques described here or by applying them to develop more advanced models to explain additional complexities such as those allosteric or linkage effects just mentioned. The target audience of this primer is the senior undergraduate or junior graduate student who lacks a foundation in ligand-binding thermodynamics. As such, we have focused primarily on foundational thermodynamic treatments and presented only general discussions of relevant experimental designs. Readers of this primer will learn how to build a working understanding of common factors that promote energetic favorability for ligand binding; develop a functional toolbox to understand ligand binding from the perspective of collecting, plotting, and interpreting ligand-binding data; enhance proficiency in deriving thermodynamic mechanisms for ligand binding; and become comfortable in interpreting binding data reported in the literature and independently expanding knowledge beyond the scope introduced in this primer."--

ISBN: 9780841299795

Standard No.: 10.1021/acsinfocus.7e7011doiSubjects--Topical Terms:

1437914
Binding free energy.
Index Terms--Genre/Form:

554714
Electronic books.

LC Class. No.: QP517.L54 / M566 2023eb

Dewey Class. No.: 572.33

National Library of Medicine Call No.: QW570 / .M56p 2023eb

Protein-ligand binding thermodynamics /
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100 1 $a Miller, Justin M., $e author. $u Middle Tennessee State University. $3 1437911
245 1 0 $a Protein-ligand binding thermodynamics / $c Justin M. Miller and Justin D. Marsee.
264 1 $a Washington, DC, USA : $b American Chemical Society, $c 2023.
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504 $a Includes bibliographical references and index.
505 0 0 $t Introduction -- $t Noncovalent Interactions Support Protein-Ligand Interactions -- $t Defining Thermodynamic Terms Used To Understand Ligand Binding Interactions -- $t Binding Polynomials and Properties of Binding Curves -- $t Common Experimental Strategies To Detect Ligand Binding -- $t Conclusion.
520 $a "Ligand binding by macromolecules represents a core event of broad relevance to a range of systems, including catalytic systems alongside noncatalytic systems such as nucleic acid binding by transcription factors or extracellular ligand binding by proteins involved in signaling pathways. The scope of this primer is constrained to introduce only foundational models without significant discussion of more advanced topics such as allosteric or linkage effects. Linkage occurs when the binding of a ligand is influenced by the binding of another molecule of the same ligand (homotropic linkage), the binding of a different ligand (heterotropic linkage), physical variables such as temperature or pressure (physical linkage), or changes in macromolecular assembly state (polysteric linkage). Taking this into account, the foundational themes presented in this primer can be used to describe any macromolecule-ligand interaction either by direct use of the models and techniques described here or by applying them to develop more advanced models to explain additional complexities such as those allosteric or linkage effects just mentioned. The target audience of this primer is the senior undergraduate or junior graduate student who lacks a foundation in ligand-binding thermodynamics. As such, we have focused primarily on foundational thermodynamic treatments and presented only general discussions of relevant experimental designs. Readers of this primer will learn how to build a working understanding of common factors that promote energetic favorability for ligand binding; develop a functional toolbox to understand ligand binding from the perspective of collecting, plotting, and interpreting ligand-binding data; enhance proficiency in deriving thermodynamic mechanisms for ligand binding; and become comfortable in interpreting binding data reported in the literature and independently expanding knowledge beyond the scope introduced in this primer."-- $c Provided by publisher.
590 $a American Chemical Society, ACS In Focus eBooks - 2023 Front Files.
650 0 $a Binding free energy. $3 1437914
650 0 $a Protein-protein interactions. $3 668549
650 0 $a Ligands (Biochemistry) $3 674516
650 0 $a Ligand binding (Biochemistry) $x Thermodynamics. $3 1437913
655 0 $a Electronic books. $2 local $3 554714
700 1 $a Marsee, Justin D., $e author. $u Middle Tennessee State University. $3 1437912
710 2 $a American Chemical Society. $3 1436935
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856 4 $u http://dx.doi.org/10.1021/acsinfocus.7e7011