The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state

Protein Engineering, Design and Selection

Volumn 23, Issue 9, 2010, Pages 729-742

  Romero Beviar, Manuel ^a   Martínez Rodríguez, Sergio ^b   Prieto, Jesús ^c   Goormaghtigh, Erik ^d   Ariz, Usue ^e,f   De la Luz Martínez Chantar, María ^e,f   Gómez, Javier ^a   Neira, José L ^a,g  

^a MIGUEL HERNÁNDEZ UNIVERSITY   (Spain)

^b UNIVERSITY OF ALMERÍA   (Spain)

^c Centro Nacional de Investigaciones Oncológicas   (Spain)

^d UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^e CIC BIOGUNE   (Spain)

^f INSTITUTO DE SALUD CARLOS III   (Spain)

^g Biocomputation and Complex Systems Physics Institute   (Spain)

Author keywords

N terminal domain; protein stability; spectroscopy; structure; unfolded state

Indexed keywords

AFFINITY VALUES; CD MEASUREMENTS; CHEMICAL DENATURATION; CIRCULAR DICHROISM; CONFORMATIONAL FREE ENERGY; CONFORMATIONAL STABILITIES; FOLDED PROTEINS; FTIR AND NMR SPECTROSCOPY; HYDROPHOBIC REGIONS; MULTI-PROTEIN COMPLEX; MULTIDOMAIN PROTEINS; N-TERMINAL DOMAINS; PH INDEPENDENT; PHOSPHOENOLPYRUVATES; PHOSPHOTRANSFERASE SYSTEM; PROTEIN STABILITY; RANDOM-COIL CONFORMATIONS; RESIDUAL STRUCTURE; SECONDARY AND TERTIARY STRUCTURES; SHEET STRUCTURE; STREPTOMYCES COELICOLOR; STRUCTURAL FEATURE; STRUCTURE; THERMAL DENATURATIONS; TWO-STATE; UNFOLDED STATE;

BINDING ENERGY; CARBOHYDRATES; DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYMES; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PHOSPHATASES; SUGAR (SUCROSE);

CONFORMATIONS;

ENZYME; ENZYME 1; HISTIDINE; UNCLASSIFIED DRUG;

ACIDITY; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME DENATURATION; HYDROPHOBICITY; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN BINDING; STREPTOMYCES COELICOLOR;

BACTERIAL PROTEINS; CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE SYSTEM; PHOSPHOTRANSFERASES (NITROGENOUS GROUP ACCEPTOR); PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STREPTOMYCES COELICOLOR; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); STREPTOMYCES COELICOLOR;

EID: 77956013701     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq045     Document Type: Article

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