Dynamic activation of protein function: a view emerging from NMR spectroscopy. Academic Article

abstract

• Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion to report on the residual conformational entropy of proteins and how this entropy can enter into both the thermodynamic and kinetic aspects of protein function.

authors

• Wand, Joshua

published proceedings

• Nat Struct Biol

author list (cited authors)

• Wand, A. J.

citation count

• 284

complete list of authors

• Wand, AJ

publication date

• November 2001

publisher

• Springer Nature  Publisher

published in

• Nature Structural and Molecular Biology  Journal

keywords

• Allosteric Regulation
• Catalysis
• ENZYMES
• Entropy
• Magnetic Resonance Spectroscopy
• Motion
• Proteins
• Structure-Activity Relationship

PubMed Central ID

• 11685236

Digital Object Identifier (DOI)

• 10.1038/nsb1101-926

start page

• 926

end page

• 931

volume

• 8

issue

• 11

URL

• http://dx.doi.org/10.1038/nsb1101-926