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Protein Secondary Structures In Water From Second-derivative Amide I Infrared Spectra.

A. Dong, P. Huang, W. Caughey
Published 1990 · Chemistry, Medicine

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Infrared spectra have been obtained for 12 globular proteins in aqueous solution at 20 degrees C. The proteins studied, which vary widely in the relative amounts of different secondary structures present, include myoglobin, hemoglobin, immunoglobulin G, concanavalin A, lysozyme, cytochrome c, alpha-chymotrypsin, trypsin, ribonuclease A, alcohol dehydrogenase, beta 2-microglobulin, and human class I major histocompatibility complex antigen A2. Criteria for evaluating how successfully the spectra due to liquid and gaseous water are subtracted from the observed spectrum in the amide I region were developed. Comparisons of second-derivative amide I spectra with available crystal structure data provide both qualitative and quantitative support for assignments of infrared bands to secondary structures. Band frequency assignments assigned to alpha-helix, beta-sheet, unordered, and turn structures are highly consistent among all proteins and agree closely with predictions from theory. alpha-Helix and unordered structures can each be assigned to only one band whereas multiple bands are associated with beta-sheets and turns. These findings demonstrate a method of analysis of second-derivative amide I spectra whereby the frequencies of bands due to different secondary structures can be obtained. Furthermore, the band intensities obtained provide a useful method for estimating the relative amounts of different structures.
This paper references
10.1016/0006-291X(83)91016-1
Protein structure by Fourier transform infrared spectroscopy: second derivative spectra.
H. Susi (1983)
10.1016/S0006-291X(88)80907-0
Infrared spectroscopy of a single cell--the human erythrocyte.
A. Dong (1988)
10.1021/BI00410A009
Solution structure of the 45-residue MgATP-binding peptide of adenylate kinase as examined by 2-D NMR, FTIR, and CD spectroscopy.
D. Fry (1988)
10.1002/BIP.360270603
Normal mode spectrum of the parallel‐chain β‐sheet
J. Bandekar (1988)
10.1016/0022-2836(77)90094-8
β-turns in proteins☆
P. Y. Chou (1977)
10.1016/0003-2697(87)90135-7
Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra.
P. Manavalan (1987)
10.1111/J.1432-1033.1987.TB13368.X
Conformational properties of azurin in solution as determined from resolution-enhanced Fourier-transform infrared spectra.
W. Surewicz (1987)
10.1007/978-94-009-9070-8
Analytical applications of FT-IR to molecular and biological systems : proceedings of the NATO Advanced Study Institute held at Florence, Italy, August 31 to September 12, 1979 [i.e. 1980]
J. Durig (1980)
10.1038/165921A0
Structure of Synthetic Polypeptides
A. Elliott (1950)
10.1038/261552a0
Structural patterns in globular proteins
M. Levitt (1976)
10.1016/0167-4838(88)90152-5
Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature.
H. L. Casal (1988)
10.1016/0005-2736(88)90210-6
Fourier transform infrared spectroscopic studies on gastric H+/K+-ATPase.
R. C. Mitchell (1988)
10.1021/JA00297A053
Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich
William T. Potter (1985)
10.1038/185422A0
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
J. Kendrew (1960)
10.1002/BIP.360250307
Examination of the secondary structure of proteins by deconvolved FTIR spectra
D. Byler (1986)
10.1016/0022-2836(77)90256-X
The structure of horse methaemoglobin at 2-0 A resolution.
R. C. Ladner (1977)
10.1021/JA01464A042
The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II Bands1
T. Miyazawa (1961)
10.1016/0022-2860(85)85012-2
Applications of Infrared, Raman, and Resonance Raman Spectroscopy in Biochemistry
F. Parker (1983)
10.1016/0371-1951(59)80221-6
Multiple differentiation as a means of band sharpening
A. E. Martin (1959)
10.1016/0076-6879(86)30015-6
Resolution-enhanced Fourier transform infrared spectroscopy of enzymes.
H. Susi (1986)
10.1007/978-1-4684-1872-9_11
Hydrogen-Deuterium Exchange
F. Parker (1971)
10.1016/0167-4838(86)90314-6
Fourier transform infrared studies of ribonuclease in H2O and 2H2O solutions.
J. M. Olinger (1986)
10.1021/BI00504A006
Estimation of globular protein secondary structure from circular dichroism.
S. Provencher (1981)
10.1073/PNAS.86.7.2321
Comparison of the secondary structures of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy.
J. Gorga (1989)
10.1016/0167-4838(88)90107-0
New insight into protein secondary structure from resolution-enhanced infrared spectra.
W. Surewicz (1988)
10.1021/AC00232A034
Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours
J. Kauppinen (1981)
10.1021/bi00508a007
Information content in the circular dichroism of proteins.
J. P. Hennessey (1981)
10.1016/S0065-3233(08)60528-8
Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins.
S. Krimm (1986)
10.1016/0003-2697(78)90812-6
Circular dichroic analysis of protein conformation: Inclusion of the β-turns☆
C. T. Chang (1978)
10.1038/329506A0
Structure of the human class I histocompatibility antigen, HLA-A2
P. Bjorkman (1987)
10.1366/0003702814732634
Fourier Self-Deconvolution: A Method for Resolving Intrinsically Overlapped Bands
J. Kauppinen (1981)
10.1016/S0065-3233(08)60520-3
The anatomy and taxonomy of protein structure.
J. S. Richardson (1981)
10.1016/0167-4838(88)90125-2
The solution structure of concanavalin A probed by FT-IR spectroscopy.
J. L. Arrondo (1988)
10.1063/1.1742489
Characteristic Infrared Bands of Monosubstituted Amides
T. Miyazawa (1956)
10.1016/0022-2836(80)90282-X
Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism.
S. Brahms (1980)
10.1016/0005-2795(73)90350-4
Chain reversals in proteins.
P. N. Lewis (1973)
10.1002/BIP.1968.360061006
Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
C. Venkatachalam (1968)
10.1366/0003702854248917
Protein Conformation by Infrared Spectroscopy: Resolution Enhancement by Fourier Self-Deconvolution
Wang-Jih Yang (1985)
10.1021/BI00429A002
Structure of cytochrome b5 in solution by Fourier-transform infrared spectroscopy.
P. E. Holloway (1989)
10.1016/0167-4838(86)90024-5
A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S.
P. Haris (1986)
10.1016/0022-2836(77)90207-8
Automatic identification of secondary structure in globular proteins.
M. Levitt (1977)
10.1021/BI00772A015
Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion.
Y. Chen (1972)
10.1021/BI00838A031
Computed circular dichroism spectra for the evaluation of protein conformation.
N. Greenfield (1969)



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10.1007/s11694-019-00139-y
Bacterial enzyme based spectrophotometric determination of phthalate esters in drinking water stored in PET bottles
A. Jayshree (2019)
10.1002/BSPY.350010602
FT‐IR spectroscopic studies on molecular interactions of cryoprotectant agents with bacteria
W. Zeroual (1995)
10.1016/S0141-8130(98)00052-X
Molecular basis of film formation from a soybean protein: comparison between the conformation of glycinin in aqueous solution and in films.
M. Subirade (1998)
10.1002/JPS.20014
Raman spectroscopic characterization of drying-induced structural changes in a therapeutic antibody: correlating structural changes with long-term stability.
Samir U. Sane (2004)
10.1016/J.IJBIOMAC.2004.09.005
Binding of genistein to human serum albumin demonstrated using tryptophan fluorescence quenching.
Qingquan Bian (2004)
10.1016/J.BBAGEN.2004.06.021
Interactions of human serum albumin with chlorogenic acid and ferulic acid.
J. Kang (2004)
10.1002/JPS.20258
Effects of benzyl alcohol on aggregation of recombinant human interleukin-1-receptor antagonist in reconstituted lyophilized formulations.
S. Roy (2005)
10.1002/BIP.20561
Solvent-induced lysozyme gels: effects of system composition and temperature on structural and dynamic characteristics.
M. A. da Silva (2006)
10.1163/156856207782246786
Nano-TiO2 induced secondary structural transition of silk fibroin studied by two-dimensional Fourier-transform infrared correlation spectroscopy and Raman spectroscopy
X. Feng (2007)
10.1007/s11095-007-9271-y
New Insight into the Role of Polyethylene Glycol Acting as Protein Release Modifier in Lipidic Implants
S. Herrmann (2007)
10.1002/JPS.20508
High concentration formulation feasibility of human immunoglubulin G for subcutaneous administration.
Bhas A. Dani (2007)
10.1016/J.MOLSTRUC.2008.12.047
Studies on the binding of a carditionic agent to human serum albumin by two-dimensional correlation fluorescence spectroscopy and molecular modeling
T. Wang (2009)
10.1016/J.IJPHARM.2008.12.018
Conformational and bioactivity analysis of insulin: freeze-drying TBA/water co-solvent system in the presence of surfactant and sugar.
Z. Yong (2009)
10.1016/J.JCT.2012.11.009
Application of molecular modelling and spectroscopic approaches for investigating the binding of tanshinone IIA to human serum albumin
Jinghong Li (2013)
10.1380/JSSSJ.29.558
表面赤外分光法を用いた抗原抗体反応の非標識検出:二次構造解析による特異・非特異信号の識別
愛弓 平野 (2008)
10.1208/ps050210
Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
J. Andya (2008)
FTIR ANALYSIS OF PROTEIN SECONDARY STRUCTURE IN SOLID AND SOLUTION STATES
Z. Pietralik (2012)
Title Hydrophobic Nanoparticles Reduce the β-Sheet Content of SEVI Amyloid Fibrils and Inhibit SEVI-Enhanced HIV Infectivity Permalink
Lauren R Brooks (2017)
2-10 μm Mid-infrared Supercontinuum Light Sources
Christian R Petersen (2016)
10.1039/c0nr00436g
Investigating the structural biofunctionality of antibodies conjugated to magnetic nanoparticles.
Emanuela Occhipinti (2011)
10.1016/0076-6879(93)26014-Z
Fourier transform infrared spectroscopy.
J. A. Larrabee (1993)
10.1016/0022-2860(93)07929-Q
Protein secondary structure of the photosystem II complex studied by FT-IR spectroscopy. Changes in the amide I region mediated by digalactosyldiacylglycerol and divalent cations
A. Menikh (1994)
10.1002/BIP.360340215
Rheological properties and conformational states of β‐conglycinin gels at acidic pH
Takao Nagano (1994)
10.1007/978-1-4615-1863-1_9
Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds.
E. Goormaghtigh (1994)
10.1002/tcr.201500272
Three-Dimensional Tissue Models Constructed by Cells with Nanometer- or Micrometer-Sized Films on the Surfaces.
C. Liu (2016)
10.1155/2012/970369
Electromagnetic Fields Effects on the Secondary Structure of Lysozyme and Bioprotective Effectiveness of Trehalose
E. Calabrò (2012)
10.1021/la4044649
Ultrathin gold nanoribbons synthesized within the interior cavity of a self-assembled peptide nanoarchitecture.
Kin-ya Tomizaki (2014)
10.1007/s10989-011-9278-4
The Role of Pro, Gly Lys, and Arg Containing Peptides on Amyloid-Beta Aggregation
Seema Jagota (2011)
10.3233/BME-161567
Attachment and conformational changes of collagen on bioactive glass surface.
K. Magyari (2016)
10.1016/j.ijbiomac.2018.11.220
Agarose-chitosan hydrogel-immobilized horseradish peroxidase with sustainable bio-catalytic and dye degradation properties.
M. Bilal (2019)
10.1039/c9cp01128e
Lysozyme-luteolin binding: molecular insights into the complexation process and the inhibitory effects of luteolin towards protein modification.
Sourav Das (2019)
10.1016/j.ijpharm.2019.02.006
Correlating multidimensional short‐term empirical protein properties to long‐term protein physical stability data via empirical phase diagrams
Marieke E Klijn (2019)
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