Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands

Infrared spectra of the amino acid residues in H2O solution have been obtained in the 1800–1400‐cm−1 region. It has been established that amino acid residues of arginine, asparagine, glutamine, aspartic and glutamic acids, lysine, tyrosine, histidine, and phenylalanine have intensive absorption in this spectral region. Infrared spectra for a set of model compounds have been measured. On the basis of these data, spectral parameters of amino acid residue absorption bands have been determined.

[1]  T. Miyazawa.  Perturbation Treatment of the Characteristic Vibrations of Polypeptide Chains in Various Configurations , 1960 .

[2]  S. Venyaminov,et al.  A structural study of filamin, a high-molecular-weight actin-binding protein from chicken gizzard. , 1982, European journal of biochemistry.

[3]  O. Fedorov,et al.  Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy water , 1975, Biopolymers.

[4]  M. Metsis,et al.  Distribution of secondary structure along the fibronectin molecule. , 1983, European journal of biochemistry.

[5]  D. Chapman,et al.  Second-derivative infrared spectroscopic studies of the secondary structures of bacteriorhodopsin and Ca2+-ATPase. , 1985, Biochemistry.

[6]  S. Venyaminov,et al.  Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random forms , 1973, Biopolymers.

[7]  V. Filimonov,et al.  A study of the structure of fibronectin. , 1981, European journal of biochemistry.

[8]  N. Nevskaya,et al.  Infrared spectra and resonance interactions of amide‐I and II vibrations of α‐helix , 1976 .

[9]  S. Venyaminov,et al.  Absence of gross changes in the secondary structure of actin at G‐F transition , 1980, FEBS letters.

[10]  L. Jaenicke.  A rapid micromethod for the determination of nitrogen and phosphate in biological material. , 1974, Analytical biochemistry.

[11]  A. Savitzky,et al.  Smoothing and Differentiation of Data by Simplified Least Squares Procedures. , 1964 .

[12]  Boris V. Shfstopalov,et al.  Quantitative Study of Secondary Structure of Histones H1, H2A, and H4 in Solution by Infrared Spectroscopy , 1976 .

[13]  H. Susi,et al.  Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.

[14]  Warren L. Butler,et al.  HIGHER DERIVATIVE ANALYSIS OF COMPLEX ABSORPTION SPECTRA , 1970 .

[15]  N. Nevskaya,et al.  Infrared spectra and resonance interaction of amide‐I vibration of the antiparallel‐chain pleated sheet , 1976, Biopolymers.

[16]  L. J. Bellamy.  The infra-red spectra of complex molecules , 1962 .

[17]  A Wlodawer,et al.  The refined crystal structure of ribonuclease A at 2.0 A resolution. , 1982, The Journal of biological chemistry.