Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions

Methods

Volumn 59, Issue 3, 2013, Pages 301-315

  Seidel, Susanne A I ^a   Dijkman, Patricia M ^b   Lea, Wendy A ^c   van den Bogaart, Geert ^e   Jerabek Willemsen, Moran ⁱ   Lazic, Ana ⁱ   Joseph, Jeremiah S ^f   Srinivasan, Prakash ^d   Baaske, Philipp ⁱ   Simeonov, Anton ^c   Katritch, Ilia ^f   Melo, Fernando A ^g   Ladbury, John E ^g   Schreiber, Gideon ^h   Watts, Anthony ^b   Braun, Dieter ^a   Duhr, Stefan ⁱ  

^a UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^e RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^f SCRIPPS RESEARCH INSTITUTE   (United States)

^g UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

^h WEIZMANN INSTITUTE OF SCIENCE   (Israel)

ⁱ NanoTemper Technologies GmbH   (Germany)

Author keywords

Binding affinity; Bioliquids; Cooperativity; Dimerization; Label free; Microscale thermophoresis

Indexed keywords

ADENOSINE A2A RECEPTOR; HISTONE METHYLTRANSFERASE; MEMBRANE PROTEIN; NEUROTENSIN RECEPTOR; SYNAPTOTAGMIN I; BETA LACTAMASE; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; HISTONE LYSINE METHYLTRANSFERASE; NEUROTENSIN TYPE 1 RECEPTOR; PROTEIN; PROTOZOAL PROTEIN;

CELL LYSATE; DIMERIZATION; HYDRATION; MICROSCALE THERMOPHORESIS; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; REVIEW; SIGNAL NOISE RATIO; ANIMAL; BINDING COMPETITION; CHEMISTRY; CONFORMATION; DRUG ANTAGONISM; LASER; METHODOLOGY; RAT; SPECTROFLUOROMETRY; TEMPERATURE; THERMODYNAMICS;

ANIMALS; BETA-LACTAMASES; BINDING, COMPETITIVE; DIMERIZATION; GRB2 ADAPTOR PROTEIN; HISTONE-LYSINE N-METHYLTRANSFERASE; LASERS; MOLECULAR CONFORMATION; PROTEIN BINDING; PROTEINS; PROTOZOAN PROTEINS; RATS; RECEPTOR, ADENOSINE A2A; RECEPTORS, NEUROTENSIN; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS;

EID: 84884497350     PISSN: 10462023     EISSN: 10959130     Source Type: Journal    
DOI: 10.1016/j.ymeth.2012.12.005     Document Type: Review

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