Comparative analysis of the packing topology of structurally important residues in helical membrane and soluble proteins

Protein Engineering, Design and Selection

Volumn 22, Issue 2, 2009, Pages 67-73

  Pabuwal, Vagmita ^a   Li, Zhijun ^a,b  

^a UNIVERSITY OF THE SCIENCES   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Hub residue; Membrane protein; Network; Residue packing

Indexed keywords

AMINO ACID RESIDUES; COMPARATIVE ANALYSIS; COMPUTATIONAL TOOLS; DEGREE OF CONNECTIVITIES; FOLDED STRUCTURES; HELICAL MEMBRANES; HIGH QUALITIES; HUB-RESIDUE; MEMBRANE PROTEIN; NETWORK; NETWORK ANALYSIS; PROTEIN STRUCTURES; RESIDUE PACKING; SOLUBLE PROTEINS; STRUCTURE PREDICTIONS; STRUCTURE-FUNCTION MODELS; THREE-DIMENSIONAL STRUCTURES; TRANS-MEMBRANE PROTEINS;

AMINES; AMINO ACIDS; ELECTRIC NETWORK ANALYSIS; MEMBRANES; ORGANIC ACIDS; THREE DIMENSIONAL; TOPOLOGY;

PROTEINS;

AMINO ACID; MEMBRANE PROTEIN; PROTEIN;

ARTICLE; BINDING SITE; COMPARATIVE STUDY; CONTROLLED STUDY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; RESIDUE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACIDS; DATA INTERPRETATION, STATISTICAL; DATABASES, PROTEIN; MEMBRANE PROTEINS; MODELS, MOLECULAR; PHYSICOCHEMICAL PHENOMENA; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SOLUBILITY; SOLVENTS;

EID: 60449097068     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn074     Document Type: Article

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