Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein.

doi:10.1006/jmbi.1994.1452

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Article

Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein.

Journal of molecular biology - 22 Jul 1994

Kim D, Kim C, Park C

Abstract excerpt

Ribose-binding protein (RBP) consists of two alpha/beta globular units; the N domain being composed of four helices (I, II, III and IX) and six sheets (A, B, C, D, E and K), and the C domain with five helices (IV, V, VI, VII and VIII) and six sheets (F, G, H, I, J and L). The two domains are conn...

Topics

Carrier Proteins
Circular Dichroism
Escherichia coli
Escherichia coli Proteins
Kinetics
Models, Molecular
Mutation
Periplasmic Binding Proteins
Protein Engineering
Protein Folding
Ribose
Spectrometry, Fluorescence
Tyrosine

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