Photoreactive stapled peptides to identify and characterize bcl-2 family interaction sites by mass spectrometry

Methods in Enzymology

Volumn 544, Issue , 2014, Pages 25-48

  Lee, Susan ^a,b   Braun, Craig R ^a,b,c   Bird, Gregory H ^a,b   Walensky, Loren D ^a,b  

^a DANA FARBER CANCER INSTITUTE   (United States)

^b BOSTON CHILDREN S HOSPITAL   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Apoptosis; BAD; BAK; BAX; BCL 2 family; BCL XL; BH3; BID; BIM; Binding site; Glucokinase; Mass spectrometry; MCL 1; Photoaffinity labeling; Photoreactive; Protein interaction; PUMA; Stabilized Alpha Helix (SAH); Stabilized Alpha Helix of BCL 2 domain (SAHB); Stapled peptide

Indexed keywords

BH3 PROTEIN; PEPTIDE; PHOTOREACTIVE STAPLED PEPTIDE; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PUMA PROTEIN; REAGENT; UNCLASSIFIED DRUG; PHOTOSENSITIZING AGENT;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; FLUORESCENCE POLARIZATION; GEL PERMEATION CHROMATOGRAPHY; HYDROPHILICITY; HYDROPHOBICITY; MASS SPECTROMETRY; METHODOLOGY; MOLECULAR DOCKING; NUCLEAR MAGNETIC RESONANCE; PEPTIDE MAPPING; PEPTIDE SYNTHESIS; PHOTOAFFINITY LABELING; PHOTOREACTIVITY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; ULTRAVIOLET RADIATION; X RAY CRYSTALLOGRAPHY; ANIMAL; APOPTOSIS; CHEMICAL STRUCTURE; HUMAN; METABOLISM; MOLECULAR GENETICS; PROCEDURES; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEOMICS;

AMINO ACID SEQUENCE; ANIMALS; APOPTOSIS; BINDING SITES; HUMANS; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOTOSENSITIZING AGENTS; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEOMICS; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 84903464142     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-417158-9.00002-9     Document Type: Chapter

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