Probing the origin of structural stability of single and double stapled p53 peptide analogs bound to MDM2

Chemical Biology and Drug Design

Volumn 83, Issue 6, 2014, Pages 631-642

  Guo, Zuojun ^a,b   Streu, Kristina ^a   Krilov, Goran ^c   Mohanty, Udayan ^a  

^a BOSTON COLLEGE   (United States)

^b GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION   (United States)

^c SCHRÖDINGER INC   (United States)

Author keywords

conformation population; contact map; end to end distance; native contact; potential of mean forces; stapled peptide; WaterMap

Indexed keywords

ALKENE; HYDROCARBON; PEPTIDE DERIVATIVE; PROTEIN MDM2; PROTEIN P53; MOLECULAR PROBE; PROTEIN BINDING;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CHEMICAL BOND; COMPLEX FORMATION; DENSITY; FORCE; HISTOGRAM; HYDRATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; STEREOCHEMISTRY; TUMOR SUPPRESSOR GENE; CHEMISTRY; METABOLISM; MOLECULAR DYNAMICS; MOLECULAR PROBE;

MOLECULAR DYNAMICS SIMULATION; MOLECULAR PROBES; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS C-MDM2; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84896286645     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/cbdd.12284     Document Type: Article

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