Results 211 to 220 of about 181,206 (262)

Conformational stability of dinucleotides in solution

Journal of Molecular Biology, 1967
Abstract A variety of 3′ → 5′ and 2′ → 5′ dinucleoside phosphates (at neutral pH) have been studied using circular dichroic and absorption spectra in a range of temperature of −20 to + 80 °C. Two kinds of circular dichroic spectra can be observed at low temperature: one “conservative” represented by a pair of bands of opposite sign, the other “non ...
J, Brahms, J C, Maurizot, A M, Michelson
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CONFORMATIONAL STABILITY OF A SNAKE CARDIOTOXIN

International Journal of Peptide and Protein Research, 1977
A snake cardiotoxin from the venom of the Formosan cobra, Naja naja atra, is a basic polypeptide. The protein can be denatured in 6.0 M guanidine hydrochloride or at elevated temperatures. Its conformation remains virtually the same in solvents of lower polarity than water such as 1, 2‐ethanediol or 1‐propanol and 1, 2‐ethanediol (1:1 v/v).
M C, Hung, Y H, Chen
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Conformational stability of a human cryoglobulin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1979
Studies on a single component human cryoimmunoglobulin (cryo-IgG) (gamma 1 : lambda, Gm 4) were undertaken to gain a better understanding of the conformational stability of macromolecular interfaces essential for self-association of cryo-IgG leading to the formation of visible gel mass.
P, Chowdhury, A, Saha
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Conformational stability of spectrin and fodrin

International Journal of Biological Macromolecules, 1989
The conformational stability of erythrocyte spectrin and brain spectrin-like protein (fodrin) has been studied by circular dichroism. In agreement with previous reports the circular dichroism spectra of both proteins in the peptide region were almost identical. The essential differences, on the other hand, were found in the near u.v.
M, Kodícek, T, Marik, K, Dobrovský
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Insights on the conformational stability of collagen

Natural Product Reports, 2001
This review describes work on the conformational stability of the collagen triple helix. In 1994, the structure of collagen was determined at high resolution. Since then, much work has been done on synthetic mimics of collagen that contain host-guest peptides, tethers, peptoid residues, or analogs of the prevalent 4(R)-hydroxy-L-proline residues.
Cara L, Jenkins, Ronald T, Raines
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Conformational Stability of Heme Proteins in vacuo

Biochemistry, 1994
The function and conformational stability of myoglobin were studied in vacuo by using an electrospray mass spectrometer. The electrospray technique gently transfers protein molecules from the solution phase to the gas phase, and solvent-free protein ions are produced in the mass spectrometer.
Konishi, Yasuo, Feng, Rong
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Conformational stability of globular proteins

Trends in Biochemical Sciences, 1990
The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
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Conformational stability of citraconylated ovalbumin

International Journal of Biochemistry, 1991
The lysine residues were modified to varying degrees (50-91%) with citraconic anhydride to determine the extent of conformational change in ovalbumin. Major findings included: 1. Sixteen of the 20 lysine residues are located on the protein surface, while the remaining four are buried. 2.
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Conformational Stability of (+)-Epichlorohydrin

The Journal of Physical Chemistry A, 2000
Vibrational absorption and circular dichroism spectra of (+)-epichlorohydrin have been recorded for the neat liquid and in organic solvents CCl4, CS2, CHCl3, CH2Cl2, and CH3I. These spectra are compared with the ab initio predictions of absorption and vibrational circular dichroism (VCD) spectra obtained with density functional theory using the B3LYP/6-
Feng Wang, Prasad L. Polavarapu
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Solvent Effects and Conformational Stability of a Tripeptide

2006
In this work we are trying to gain an insight on the molecular mechanisms of the salt effects on conformational stability of proteins with use of fully atomistic Molecular Dynamics simulations techniques. Such ‘in silico’ approach allows us to obtain quite realistic data on the time and scale resolutions that are unavailable for both ‘in vitro’ and ‘in
Maxim V. Fedorov, Stephan Schumm, Jonathan M. Goodman   +2 more
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