+353-1-416-8900REST OF WORLD
+44-20-3973-8888REST OF WORLD
1-917-300-0470EAST COAST U.S
1-800-526-8630U.S. (TOLL FREE)


Peptide Solvation and H-bonds, Vol 72. Advances in Protein Chemistry

  • ID: 1769293
  • Book
  • 312 Pages
  • Elsevier Science and Technology
1 of 3
Volume 72, Peptide Solvation and H-bonds, addresses the role of peptide backbone solvation in the energetics of protein folding. Particular attention is focused on modeling and computation. This volume will be of particular interest to biophysicists and structural biologists.

- Challenges the longstanding and basic assumptions of structural biology- Discusses how to solve the problem of protein structure prediction- Addresses the quantitation of the energetics of folding

Please Note: This is an On Demand product, delivery may take up to 11 working days after payment has been received.
Note: Product cover images may vary from those shown
2 of 3
Preface: New Directions in the Study of Peptide H-bonds and Peptide Solvation; Potential Functions for Hydrogen Bonds in Protein Structure Prediction and Design; Backbone-Backbone H-Bonds Make Context Dependent Contributions to Protein Folding Kinetics and Thermodynamics: Lessons from Amide-to-Ester Mutations; Modeling Polarization in Proteins and Protein-Ligand Complexes: Methods and Preliminary Results; Hydrogen Bonds in Molecular Mechanics Force Fields; Resonance Character of Hydrogen-Bonding Interactions in Water and Other H-Bonded Species; How Hydrogen Bonds Shape Membrane Protein Structure; Peptide and Protein Folding and Conformational Equilibria: Theoretical Treatment of Electrostatics and Hydrogen Bonding with Implicit Solvent Models; Thermodynamics of α-Helix Formation; The Importance of Cooperative Interactions and A Solid State Paradigm to Proteins
What Peptide Chemists Can Learn from Molecular Crystals
Note: Product cover images may vary from those shown
3 of 3


4 of 3
Baldwin, Robert.
Former Senior Lecturer, Willesden College of Technology, London
Baker, David James.

Note: Product cover images may vary from those shown