Annual review of biophysics and bioengineering最新文献

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Total internal reflection fluorescence. 全内反射荧光。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.001335
D Axelrod, T P Burghardt, N L Thompson
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引用次数: 736
Solid state NMR studies of protein internal dynamics. 蛋白质内部动力学的固体核磁共振研究。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.001013
D A Torchia
{"title":"Solid state NMR studies of protein internal dynamics.","authors":"D A Torchia","doi":"10.1146/annurev.bb.13.060184.001013","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001013","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"125-44"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001013","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 102
Optical sectioning microscopy: cellular architecture in three dimensions. 光学切片显微镜:三维细胞结构。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.001203
D A Agard
{"title":"Optical sectioning microscopy: cellular architecture in three dimensions.","authors":"D A Agard","doi":"10.1146/annurev.bb.13.060184.001203","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001203","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"191-219"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001203","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17795861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 505
Multifrequency phase and modulation fluorometry. 多频相位和调制荧光测定法。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.000541
E Gratton, D M Jameson, R D Hall
{"title":"Multifrequency phase and modulation fluorometry.","authors":"E Gratton, D M Jameson, R D Hall","doi":"10.1146/annurev.bb.13.060184.000541","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.000541","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"105-24"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.000541","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437417","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 273
Amino acid, peptide, and protein volume in solution. 氨基酸、肽和蛋白质在溶液中的体积。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.001045
A A Zamyatnin
{"title":"Amino acid, peptide, and protein volume in solution.","authors":"A A Zamyatnin","doi":"10.1146/annurev.bb.13.060184.001045","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001045","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"145-65"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001045","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 235
NMR studies of intracellular metal ions in intact cells and tissues. 完整细胞和组织中细胞内金属离子的核磁共振研究。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.001253
R K Gupta, P Gupta, R D Moore
{"title":"NMR studies of intracellular metal ions in intact cells and tissues.","authors":"R K Gupta, P Gupta, R D Moore","doi":"10.1146/annurev.bb.13.060184.001253","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001253","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"221-46"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001253","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 188
Detailed analysis of protein structure and function by NMR spectroscopy: survey of resonance assignments. 核磁共振波谱法对蛋白质结构和功能的详细分析:共振分配的调查。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.002425
J L Markley, E L Ulrich
{"title":"Detailed analysis of protein structure and function by NMR spectroscopy: survey of resonance assignments.","authors":"J L Markley,&nbsp;E L Ulrich","doi":"10.1146/annurev.bb.13.060184.002425","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002425","url":null,"abstract":"<p><p>Techniques are now available for making extensive assignments in NMR spectra of proteins of moderate size (molecular weight 20,000 or less). Such assignments provide the first step for experiments designed to extract the full complement of NMR parameters for each group in a protein. The stage is set for exciting research scenarios in protein chemistry involving, for example, the determination of hydrogen exchange kinetics at all exchangeable positions whose half times are on the order of 100 ms (277) or longer than a few minutes (316, 569, 570); the characterization of intermediates in protein folding pathways (318); measurement of the distribution of internal motions within a protein molecule (573); a detailed description of the biophysical consequences of single amino acid replacements in small proteins (387); elucidation of the mechanisms of conformational transitions in proteins; and multiparametric characterization of the parts of an enzyme that participate in catalytic mechanisms. Small proteins for which extensive 1H NMR assignments have been made include lysozyme, several cytochromes, ferredoxins, myelin basic proteins, PTI and related proteinase inhibitors, proteinase inhibitors from seminal plasma and avian eggs, apamin, and several snake venom neurotoxins. (References are given in Table 1).</p>","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"493-521"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002425","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17391708","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 13
Evolution and the tertiary structure of proteins. 蛋白质的进化和三级结构。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.002321
M Bajaj, T Blundell
{"title":"Evolution and the tertiary structure of proteins.","authors":"M Bajaj,&nbsp;T Blundell","doi":"10.1146/annurev.bb.13.060184.002321","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002321","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"453-92"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002321","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437426","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 156
The Na/K pump of cardiac cells. 心脏细胞的钠钾泵。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.002105
D C Gadsby
{"title":"The Na/K pump of cardiac cells.","authors":"D C Gadsby","doi":"10.1146/annurev.bb.13.060184.002105","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002105","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"373-98"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002105","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17391707","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 98
Sequence-determined DNA separations. 序列确定的DNA分离。
Annual review of biophysics and bioengineering Pub Date : 1984-01-01 DOI: 10.1146/annurev.bb.13.060184.002151
L S Lerman, S G Fischer, I Hurley, K Silverstein, N Lumelsky
{"title":"Sequence-determined DNA separations.","authors":"L S Lerman,&nbsp;S G Fischer,&nbsp;I Hurley,&nbsp;K Silverstein,&nbsp;N Lumelsky","doi":"10.1146/annurev.bb.13.060184.002151","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002151","url":null,"abstract":"<p><p>The variation in electrophoretic mobility of DNA under conditions of marginal helix stability provides a useful means for investigation of the relation between the helix-random chain transition and base sequence in natural DNA and a powerful procedure for separation of DNA molecules according to sequence. The use of statistical mechanical theory for analysis of the transition equilibria together with new, simplified theoretical considerations on the effect of strand unravelling on mobility have shown that the gel behavior is predictable for known sequences. A number of the distinctive consequences of the theory and their correspondence with the properties of real molecules have been demonstrated. These include the extremely close cooperative linkage of large blocks of bases into domains, the existence of sharp boundaries between domains, the major role of nearest-neighbor interaction in determining stability, the dependence of domain structures on neighboring and more remote sequences, and the depression of domain melting temperature if the sequence lies at the end of a molecule. New and unusual applications derive from the possibility of separating DNA molecules by properties of their sequence. Exceedingly complex mixtures, such as the sum of all fragments produced by the action of a sixbase specific restriction endonuclease on a complete bacterial genome, can be resolved completely. Additional inserted sequences are easily discerned. The difference of a single base pair in a molecule permits detection and isolation of mutant sequences. The need for full sequential analysis of long molecules for characterization of mutants can be reduced by localizing a change within a small fragment.</p>","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"399-423"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002151","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17297931","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 182
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