Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme
about
Identification of compact, hydrophobically stabilized domains and modules containing multiple peptide chainsSperm Lysozyme-Like Protein 1 (SLLP1), an intra-acrosomal oolemmal-binding sperm protein, reveals filamentous organization in protein crystal form.A quality metric for homology modeling: the H-factor.Functional region prediction with a set of appropriate homologous sequences--an index for sequence selection by integrating structure and sequence information with spatial statistics.The perturbations of the native state of goat alpha-lactalbumin induced by 1,1'-bis(4-anilino-5-naphthalenesulfonate) are Ca2+-dependentLow resolution solution structure of HAMLET and the importance of its alpha-domains in tumoricidal activity.Temperature dependence of the phosphorescence quantum yield of various alpha-lactalbumins and of hen egg-white lysozyme.Mutations in the K+ channel signature sequence.Analysis of alphalactalbumin and betalactoglobulin from the rehydration of bovine colostrum powder using cloud point extraction and mass spectrometryFK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules.Automatic recognition of hydrophobic clusters and their correlation with protein folding unitsEnergetics of structural domains in alpha-lactalbumin.Fluorescence correlation spectroscopy study of protein transport and dynamic interactions with clustered-charge peptide adsorbents.Functional conversion of the homologous proteins alpha-lactalbumin and lysozyme by exon exchangeGuiding protein aggregation with macromolecular crowdingStructural basis for difference in heat capacity increments for Ca(2+) binding to two alpha-lactalbumins.Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin.Membrane-bound states of alpha-lactalbumin: implications for the protein stability and conformation.Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.Calcium-binding and structural stability of echidna and canine milk lysozymes.Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability.Stability of HAMLET--a kinetically trapped alpha-lactalbumin oleic acid complex.
P2860
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P2860
Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme
description
1989 nî lūn-bûn
@nan
1989 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Refined structure of baboon al ...... omparison with C-type lysozyme
@ast
Refined structure of baboon al ...... omparison with C-type lysozyme
@en
Refined structure of baboon al ...... omparison with C-type lysozyme
@nl
type
label
Refined structure of baboon al ...... omparison with C-type lysozyme
@ast
Refined structure of baboon al ...... omparison with C-type lysozyme
@en
Refined structure of baboon al ...... omparison with C-type lysozyme
@nl
prefLabel
Refined structure of baboon al ...... omparison with C-type lysozyme
@ast
Refined structure of baboon al ...... omparison with C-type lysozyme
@en
Refined structure of baboon al ...... omparison with C-type lysozyme
@nl
P2093
P1476
Refined structure of baboon al ...... omparison with C-type lysozyme
@en
P2093
D C Phillips
D I Stuart
K R Acharya
N P Walker
P304
P407
P577
1989-07-05T00:00:00Z