Proton transfer and polarizability of hydrogen bonds in proteins coupled with conformational changes. I. Infrared investigation of poly(glutamic acid) with various N Bases
- 1 November 1977
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 16 (11) , 2407-2418
- https://doi.org/10.1002/bip.1977.360161106
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Polarizability, proton transfer and symmetry of energy surfaces of carboxylic acid—N-base hydrogen bonds. Infrared investigationsJournal of the Chemical Society, Faraday Transactions 2: Molecular and Chemical Physics, 1977
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- The Crystal and Molecular Structure of DIP-inhibited Bovine Trypsin at 2.7A ResolutionPublished by Cold Spring Harbor Laboratory ,1972
- On the Mechanism of Action of Ribonuclease T1European Journal of Biochemistry, 1971
- Applications of Infrared Spectroscopy in Biochemistry, Biology, and MedicinePublished by Springer Nature ,1971
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Models of intermolecular interactions involving proton transfer in biopolymersBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Three-dimensional Structure of Tosyl-elastaseNature, 1970
- Proton magnetic resonance studies on ribonuclease T1Biochemical and Biophysical Research Communications, 1969
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969