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circular dichroism (17) 17
biochemistry & molecular biology (15) 15
protein structure, secondary (13) 13
animals (8) 8
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globular-proteins (6) 6
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Journal of food science and technology, ISSN 0022-1155, 2015, Volume 52, Issue 3, pp. 1552 - 1560
... (Phaseolus aureus) legume cultivars V. B. Sashikala & Y. N. Sreerama & V. M. Pratape & H. V. Narasimha Revised: 3 August 2013 /Accepted: 12 August 2013 /Published online... 
Green gram | Prolamines | Albumins | Cooking | Globulins | Protein solubility | FOOD SCIENCE & TECHNOLOGY | GLUTELINS | SEEDS | FRACTIONS | SCANNING-ELECTRON-MICROSCOPY | COWPEA | PHYTIC ACID | VULGARIS | DIGESTIBILITY | NUTRITIONAL QUALITY | Studies | Proteins | Legumes | Food science | Cultivars | Original
Journal Article
Protein Science, ISSN 0961-8368, 02/2003, Volume 12, Issue 2, pp. 384 - 388
Circular dichroism spectra of proteins are sensitive to protein secondary structure. The CD spectra of α‐rich proteins are similar to those of model α‐helices,... 
β‐rich proteins | Protein secondary structure | P2 structure | protein CD | β-rich proteins | Protein CD | structure | For the Record
Journal Article
Protein science, ISSN 0961-8368, 2/1999, Volume 8, Issue 2, pp. 370 - 380
Journal Article
Protein science, ISSN 1469-896X, 2004, Volume 13, Issue 1, pp. 100 - 112
Analysis of circular dichroism spectra of proteins provides information about protein secondary structure. Analytical methods developed for such an analysis... 
SP48, reference set of 48 soluble proteins | SP43, reference set of 43 soluble proteins | U, unordered | SELCON3, the self‐consistent method for protein CD analysis, version 3 | SMP50, reference set of 50 soluble + membrane proteins | RMS, root mean square | δ, RMS deviation | NRMSD, normalized RMS deviation | reference protein set | membrane proteins | α, total α‐helix | αR, regular α‐helix | SMP56, reference set of 56 soluble + membrane proteins | αD, distorted α‐helix | CCA, the convex constraint method for protein CD analysis | βR, regular β‐strand | βD, distorted β‐strand | δf, RMS deviation between the CD estimates and the crystal structure values of secondary structure fractions for a given protein | CDPro | δX, RMS deviation between the CD‐estimated and the X‐ray values of the secondary structure X for a set of proteins, X = α, β, T and U | PDB, Protein Data Bank | SP29, reference set of 29 soluble proteins | r, correlation coefficient | SP37, reference set of 37 soluble proteins | T, turns | CONTIN/LL, the ridge‐regression method for protein CD analysis combined with the locally linearized method for variable selection | CDSSTR, Johnson's minimal basis‐random selection method for protein CD analysis | MP30, reference set of 30 membrane proteins | rX, correlation between the CD‐estimated and the X‐ray values of the secondary structure X for a set of proteins, X = α, β, T and U | DSSP, a computer program for defining secondary structure of proteins | protein secondary structure | SP42, reference set of 42 soluble proteins | fX, fractional content of secondary structure X, X = α, β, T and U | MP13, reference set of 13 membrane proteins | protein CD | β, total β‐sheet | CD, circular dichroism | Protein secondary structure | Protein CD | Reference protein set | Membrane proteins | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONFORMATION | SUBUNIT C | PREDICTION | STATISTICAL-ANALYSES | DECONVOLUTION | ATP SYNTHASE | SPECTROSCOPY | NEURAL-NETWORK | INCLUSION | SECONDARY STRUCTURE | Reference Standards | Membrane Proteins - chemistry | Protein Structure, Secondary | Species Specificity | Rhodopseudomonas - chemistry | Bacterial Proteins - chemistry | Rhodobacter sphaeroides - chemistry | Solubility | Circular Dichroism | Halobacterium salinarum - chemistry | Rhodobacter capsulatus - chemistry
Journal Article
2004, ISBN 9780121827885, Volume 383
This chapter presents computation and analysis of protein circular dichroism (CD) spectra. The origins of electronic CD in proteins, theoretical methods for... 
Protein Structure, Tertiary | Absorption | Animals | Ultraviolet Rays | Protein Structure, Secondary | Proteins - radiation effects | Amino Acids - chemistry | Protein Conformation | Software | Proteins - chemistry | Circular Dichroism
Book Chapter
Biochemistry (Easton), ISSN 0006-2960, 07/1993, Volume 32, Issue 26, pp. 6674 - 6679
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 09/1999, Volume 36, Issue 4, pp. 400 - 406
A significant fraction of the so‐called “random coil” residues in globular proteins exists in the left‐handed poly(Pro)II conformation. In order to compare the... 
MD simulations | poly(Pro)II conformation | α‐helix | β‐strand | water‐bridge | Water-bridge | α-helix | β-strand
Journal Article
04/2018
The present invention provides for a novel method and apparatus for the simultaneous generation and detection of optical diffraction interference pattern on a... 
TESTING | MEASUREMENT OF MECHANICAL VIBRATIONS OR ULTRASONIC, SONIC ORINFRASONIC WAVES | MEASURING | PHYSICS
Patent
Biochemistry (Easton), ISSN 0006-2960, 1994, Volume 33, Issue 33, pp. 10022 - 10025
A method to identify poly(L-proline)-type (P-II) conformation in crystal structures of globular proteins is presented. Short segments of P-II structure were... 
SECONDARY-STRUCTURE | CONFORMATION | SPECTRA | DATA-BANK | BIOCHEMISTRY & MOLECULAR BIOLOGY | PREDICTION | Peptides - chemistry | Protein Structure, Secondary | Circular Dichroism | Crystallization
Journal Article
PROTEINS-STRUCTURE FUNCTION AND GENETICS, ISSN 0887-3585, 09/1999, Volume 36, Issue 4, pp. 400 - 406
Journal Article