Native and nonnative conformational preferences in the urea-unfolded state of barstar

Protein Science

Volumn 13, Issue 12, 2004, Pages 3085-3091

  Bhavesh, Neel S ^a   Juneja, Juhi ^b   Udgaonkar, Jayant B ^b   Hosur, Ramakrishna V ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

HN(C)N; HNN; Secondary chemical shifts; Unfolded state

Indexed keywords

BARSTAR; POLYPEPTIDE; UREA;

ARTICLE; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; ENZYME CONFORMATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ANALYSIS;

BACTERIAL PROTEINS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SOLVENTS; UREA;

EID: 9344227330     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04805204     Document Type: Article

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